data_9DYB
# 
_entry.id   9DYB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DYB         pdb_00009dyb 10.2210/pdb9dyb/pdb 
WWPDB D_1000289072 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DYB 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pagerc@miamioh.edu 
_pdbx_contact_author.name_first         Richard 
_pdbx_contact_author.name_last          Page 
_pdbx_contact_author.name_mi            C 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3006-3171 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, H.'  1 ?                   
'Nix, J.C.'  2 0000-0002-4041-4975 
'Page, R.C.' 3 0000-0002-3006-3171 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary Biorxiv                          ? ?    2692-8205 ? ? ? ? ? ? 
'Phosphorylation-State Modulated Binding of HSP70: Structural Insights and Compensatory Protein Engineering.' 2025 ? 
10.1101/2025.02.17.637997 40027613 ? ? 
? ? ? ? ? ? ? ?  ? ? 1       'Acta Crystallogr D Struct Biol' ? 0353 ?         ? ? ? ? ? ? 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix'  2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Stewart, M.'        1  ?                   
primary 'Paththamperuma, C.' 2  ?                   
primary 'McCann, C.'         3  ?                   
primary 'Cottingim, K.'      4  ?                   
primary 'Zhang, H.'          5  ?                   
primary 'DelVecchio, R.'     6  ?                   
primary 'Peng, I.'           7  ?                   
primary 'Fennimore, E.'      8  ?                   
primary 'Nix, J.C.'          9  ?                   
primary 'Saeed, M.N.'        10 ?                   
primary 'George, K.'         11 ?                   
primary 'Makaroff, K.'       12 ?                   
primary 'Colie, M.'          13 ?                   
primary 'Paulakonis, E.'     14 ?                   
primary 'Almeida, M.F.'      15 ?                   
primary 'Afolayan, A.J.'     16 ?                   
primary 'Brown, N.G.'        17 ?                   
primary 'Page, R.C.'         18 ?                   
primary 'Schisler, J.C.'     19 0000-0001-7382-2783 
1       'Liebschner, D.'     20 0000-0003-3921-3209 
1       'Afonine, P.V.'      21 0000-0002-5052-991X 
1       'Baker, M.L.'        22 ?                   
1       'Bunkoczi, G.'       23 ?                   
1       'Chen, V.B.'         24 0000-0003-2492-979X 
1       'Croll, T.I.'        25 ?                   
1       'Hintze, B.'         26 0000-0002-4871-2096 
1       'Hung, L.W.'         27 0000-0001-6690-8458 
1       'Jain, S.'           28 ?                   
1       'McCoy, A.J.'        29 ?                   
1       'Moriarty, N.W.'     30 0000-0001-8857-9464 
1       'Oeffner, R.D.'      31 0000-0003-3107-2202 
1       'Poon, B.K.'         32 0000-0001-9633-6067 
1       'Prisant, M.G.'      33 ?                   
1       'Read, R.J.'         34 0000-0001-8273-0047 
1       'Richardson, J.S.'   35 0000-0002-3311-2944 
1       'Richardson, D.C.'   36 ?                   
1       'Sammito, M.D.'      37 0000-0002-8346-9247 
1       'Sobolev, O.V.'      38 0000-0002-0623-3214 
1       'Stockwell, D.H.'    39 ?                   
1       'Terwilliger, T.C.'  40 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'   41 ?                   
1       'Videau, L.L.'       42 ?                   
1       'Williams, C.J.'     43 ?                   
1       'Adams, P.D.'        44 0000-0001-9333-8219 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'E3 ubiquitin-protein ligase CHIP' 15884.057 1   2.3.2.27 ? 'TPR domain' 
;residues "GAMGS" at N-terminus added during cloning as part of the fusion protein
;
2 polymer     syn 'Heat shock 70 kDa protein 1A'     938.870   1   3.6.1.3  ? ?            'phosphorylated threonine' 
3 non-polymer syn 'CHLORIDE ION'                     35.453    1   ?        ? ?            ? 
4 water       nat water                              18.015    144 ?        ? ?            ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Antigen NY-CO-7,CLL-associated antigen KW-8,Carboxy terminus of Hsp70-interacting protein,RING-type E3 ubiquitin transferase CHIP,STIP1 homology and U box-containing protein 1
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVK
AHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERR
;
;GAMGSEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVK
AHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERR
;
A ? 
2 'polypeptide(L)' no yes 'GP(TPO)IEEVD' GPTIEEVD B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION' CL  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   GLU n 
1 7   LYS n 
1 8   SER n 
1 9   PRO n 
1 10  SER n 
1 11  ALA n 
1 12  GLN n 
1 13  GLU n 
1 14  LEU n 
1 15  LYS n 
1 16  GLU n 
1 17  GLN n 
1 18  GLY n 
1 19  ASN n 
1 20  ARG n 
1 21  LEU n 
1 22  PHE n 
1 23  VAL n 
1 24  GLY n 
1 25  ARG n 
1 26  LYS n 
1 27  TYR n 
1 28  PRO n 
1 29  GLU n 
1 30  ALA n 
1 31  ALA n 
1 32  ALA n 
1 33  CYS n 
1 34  TYR n 
1 35  GLY n 
1 36  ARG n 
1 37  ALA n 
1 38  ILE n 
1 39  THR n 
1 40  ARG n 
1 41  ASN n 
1 42  PRO n 
1 43  LEU n 
1 44  VAL n 
1 45  ALA n 
1 46  VAL n 
1 47  TYR n 
1 48  TYR n 
1 49  THR n 
1 50  ASN n 
1 51  ARG n 
1 52  ALA n 
1 53  LEU n 
1 54  CYS n 
1 55  TYR n 
1 56  LEU n 
1 57  LYS n 
1 58  MET n 
1 59  GLN n 
1 60  GLN n 
1 61  HIS n 
1 62  GLU n 
1 63  GLN n 
1 64  ALA n 
1 65  LEU n 
1 66  ALA n 
1 67  ASP n 
1 68  CYS n 
1 69  ARG n 
1 70  ARG n 
1 71  ALA n 
1 72  LEU n 
1 73  GLU n 
1 74  LEU n 
1 75  ASP n 
1 76  GLY n 
1 77  GLN n 
1 78  SER n 
1 79  VAL n 
1 80  LYS n 
1 81  ALA n 
1 82  HIS n 
1 83  PHE n 
1 84  PHE n 
1 85  LEU n 
1 86  GLY n 
1 87  GLN n 
1 88  CYS n 
1 89  GLN n 
1 90  LEU n 
1 91  GLU n 
1 92  MET n 
1 93  GLU n 
1 94  SER n 
1 95  TYR n 
1 96  ASP n 
1 97  GLU n 
1 98  ALA n 
1 99  ILE n 
1 100 ALA n 
1 101 ASN n 
1 102 LEU n 
1 103 GLN n 
1 104 ARG n 
1 105 ALA n 
1 106 TYR n 
1 107 SER n 
1 108 LEU n 
1 109 ALA n 
1 110 LYS n 
1 111 GLU n 
1 112 GLN n 
1 113 ARG n 
1 114 LEU n 
1 115 ASN n 
1 116 PHE n 
1 117 GLY n 
1 118 ASP n 
1 119 ASP n 
1 120 ILE n 
1 121 PRO n 
1 122 SER n 
1 123 ALA n 
1 124 LEU n 
1 125 ARG n 
1 126 ILE n 
1 127 ALA n 
1 128 LYS n 
1 129 LYS n 
1 130 LYS n 
1 131 ARG n 
1 132 TRP n 
1 133 ASN n 
1 134 SER n 
1 135 ILE n 
1 136 GLU n 
1 137 GLU n 
1 138 ARG n 
1 139 ARG n 
2 1   GLY n 
2 2   PRO n 
2 3   TPO n 
2 4   ILE n 
2 5   GLU n 
2 6   GLU n 
2 7   VAL n 
2 8   ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   139 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'STUB1, CHIP, PP1131' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       8 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ?                  'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ?                  'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ?                  'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ?                  'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'   ?                  'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE         ?                  'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ?                  'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ?                  'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ?                  'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ?                  'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ?                  'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ?                  'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ?                  'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ?                  'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE       ?                  'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE    ?                  'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ?                  'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ?                  'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE        ?                  'C4 H9 N O3'     119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
TRP 'L-peptide linking' y TRYPTOPHAN       ?                  'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE         ?                  'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE           ?                  'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   16  ?   ?   ?   A . n 
A 1 2   ALA 2   17  ?   ?   ?   A . n 
A 1 3   MET 3   18  ?   ?   ?   A . n 
A 1 4   GLY 4   19  ?   ?   ?   A . n 
A 1 5   SER 5   20  ?   ?   ?   A . n 
A 1 6   GLU 6   21  ?   ?   ?   A . n 
A 1 7   LYS 7   22  ?   ?   ?   A . n 
A 1 8   SER 8   23  23  SER SER A . n 
A 1 9   PRO 9   24  24  PRO PRO A . n 
A 1 10  SER 10  25  25  SER SER A . n 
A 1 11  ALA 11  26  26  ALA ALA A . n 
A 1 12  GLN 12  27  27  GLN GLN A . n 
A 1 13  GLU 13  28  28  GLU GLU A . n 
A 1 14  LEU 14  29  29  LEU LEU A . n 
A 1 15  LYS 15  30  30  LYS LYS A . n 
A 1 16  GLU 16  31  31  GLU GLU A . n 
A 1 17  GLN 17  32  32  GLN GLN A . n 
A 1 18  GLY 18  33  33  GLY GLY A . n 
A 1 19  ASN 19  34  34  ASN ASN A . n 
A 1 20  ARG 20  35  35  ARG ARG A . n 
A 1 21  LEU 21  36  36  LEU LEU A . n 
A 1 22  PHE 22  37  37  PHE PHE A . n 
A 1 23  VAL 23  38  38  VAL VAL A . n 
A 1 24  GLY 24  39  39  GLY GLY A . n 
A 1 25  ARG 25  40  40  ARG ARG A . n 
A 1 26  LYS 26  41  41  LYS LYS A . n 
A 1 27  TYR 27  42  42  TYR TYR A . n 
A 1 28  PRO 28  43  43  PRO PRO A . n 
A 1 29  GLU 29  44  44  GLU GLU A . n 
A 1 30  ALA 30  45  45  ALA ALA A . n 
A 1 31  ALA 31  46  46  ALA ALA A . n 
A 1 32  ALA 32  47  47  ALA ALA A . n 
A 1 33  CYS 33  48  48  CYS CYS A . n 
A 1 34  TYR 34  49  49  TYR TYR A . n 
A 1 35  GLY 35  50  50  GLY GLY A . n 
A 1 36  ARG 36  51  51  ARG ARG A . n 
A 1 37  ALA 37  52  52  ALA ALA A . n 
A 1 38  ILE 38  53  53  ILE ILE A . n 
A 1 39  THR 39  54  54  THR THR A . n 
A 1 40  ARG 40  55  55  ARG ARG A . n 
A 1 41  ASN 41  56  56  ASN ASN A . n 
A 1 42  PRO 42  57  57  PRO PRO A . n 
A 1 43  LEU 43  58  58  LEU LEU A . n 
A 1 44  VAL 44  59  59  VAL VAL A . n 
A 1 45  ALA 45  60  60  ALA ALA A . n 
A 1 46  VAL 46  61  61  VAL VAL A . n 
A 1 47  TYR 47  62  62  TYR TYR A . n 
A 1 48  TYR 48  63  63  TYR TYR A . n 
A 1 49  THR 49  64  64  THR THR A . n 
A 1 50  ASN 50  65  65  ASN ASN A . n 
A 1 51  ARG 51  66  66  ARG ARG A . n 
A 1 52  ALA 52  67  67  ALA ALA A . n 
A 1 53  LEU 53  68  68  LEU LEU A . n 
A 1 54  CYS 54  69  69  CYS CYS A . n 
A 1 55  TYR 55  70  70  TYR TYR A . n 
A 1 56  LEU 56  71  71  LEU LEU A . n 
A 1 57  LYS 57  72  72  LYS LYS A . n 
A 1 58  MET 58  73  73  MET MET A . n 
A 1 59  GLN 59  74  74  GLN GLN A . n 
A 1 60  GLN 60  75  75  GLN GLN A . n 
A 1 61  HIS 61  76  76  HIS HIS A . n 
A 1 62  GLU 62  77  77  GLU GLU A . n 
A 1 63  GLN 63  78  78  GLN GLN A . n 
A 1 64  ALA 64  79  79  ALA ALA A . n 
A 1 65  LEU 65  80  80  LEU LEU A . n 
A 1 66  ALA 66  81  81  ALA ALA A . n 
A 1 67  ASP 67  82  82  ASP ASP A . n 
A 1 68  CYS 68  83  83  CYS CYS A . n 
A 1 69  ARG 69  84  84  ARG ARG A . n 
A 1 70  ARG 70  85  85  ARG ARG A . n 
A 1 71  ALA 71  86  86  ALA ALA A . n 
A 1 72  LEU 72  87  87  LEU LEU A . n 
A 1 73  GLU 73  88  88  GLU GLU A . n 
A 1 74  LEU 74  89  89  LEU LEU A . n 
A 1 75  ASP 75  90  90  ASP ASP A . n 
A 1 76  GLY 76  91  91  GLY GLY A . n 
A 1 77  GLN 77  92  92  GLN GLN A . n 
A 1 78  SER 78  93  93  SER SER A . n 
A 1 79  VAL 79  94  94  VAL VAL A . n 
A 1 80  LYS 80  95  95  LYS LYS A . n 
A 1 81  ALA 81  96  96  ALA ALA A . n 
A 1 82  HIS 82  97  97  HIS HIS A . n 
A 1 83  PHE 83  98  98  PHE PHE A . n 
A 1 84  PHE 84  99  99  PHE PHE A . n 
A 1 85  LEU 85  100 100 LEU LEU A . n 
A 1 86  GLY 86  101 101 GLY GLY A . n 
A 1 87  GLN 87  102 102 GLN GLN A . n 
A 1 88  CYS 88  103 103 CYS CYS A . n 
A 1 89  GLN 89  104 104 GLN GLN A . n 
A 1 90  LEU 90  105 105 LEU LEU A . n 
A 1 91  GLU 91  106 106 GLU GLU A . n 
A 1 92  MET 92  107 107 MET MET A . n 
A 1 93  GLU 93  108 108 GLU GLU A . n 
A 1 94  SER 94  109 109 SER SER A . n 
A 1 95  TYR 95  110 110 TYR TYR A . n 
A 1 96  ASP 96  111 111 ASP ASP A . n 
A 1 97  GLU 97  112 112 GLU GLU A . n 
A 1 98  ALA 98  113 113 ALA ALA A . n 
A 1 99  ILE 99  114 114 ILE ILE A . n 
A 1 100 ALA 100 115 115 ALA ALA A . n 
A 1 101 ASN 101 116 116 ASN ASN A . n 
A 1 102 LEU 102 117 117 LEU LEU A . n 
A 1 103 GLN 103 118 118 GLN GLN A . n 
A 1 104 ARG 104 119 119 ARG ARG A . n 
A 1 105 ALA 105 120 120 ALA ALA A . n 
A 1 106 TYR 106 121 121 TYR TYR A . n 
A 1 107 SER 107 122 122 SER SER A . n 
A 1 108 LEU 108 123 123 LEU LEU A . n 
A 1 109 ALA 109 124 124 ALA ALA A . n 
A 1 110 LYS 110 125 125 LYS LYS A . n 
A 1 111 GLU 111 126 126 GLU GLU A . n 
A 1 112 GLN 112 127 127 GLN GLN A . n 
A 1 113 ARG 113 128 128 ARG ARG A . n 
A 1 114 LEU 114 129 129 LEU LEU A . n 
A 1 115 ASN 115 130 130 ASN ASN A . n 
A 1 116 PHE 116 131 131 PHE PHE A . n 
A 1 117 GLY 117 132 132 GLY GLY A . n 
A 1 118 ASP 118 133 133 ASP ASP A . n 
A 1 119 ASP 119 134 134 ASP ASP A . n 
A 1 120 ILE 120 135 135 ILE ILE A . n 
A 1 121 PRO 121 136 136 PRO PRO A . n 
A 1 122 SER 122 137 137 SER SER A . n 
A 1 123 ALA 123 138 138 ALA ALA A . n 
A 1 124 LEU 124 139 139 LEU LEU A . n 
A 1 125 ARG 125 140 140 ARG ARG A . n 
A 1 126 ILE 126 141 141 ILE ILE A . n 
A 1 127 ALA 127 142 142 ALA ALA A . n 
A 1 128 LYS 128 143 143 LYS LYS A . n 
A 1 129 LYS 129 144 144 LYS LYS A . n 
A 1 130 LYS 130 145 145 LYS LYS A . n 
A 1 131 ARG 131 146 146 ARG ARG A . n 
A 1 132 TRP 132 147 147 TRP TRP A . n 
A 1 133 ASN 133 148 148 ASN ASN A . n 
A 1 134 SER 134 149 149 SER SER A . n 
A 1 135 ILE 135 150 150 ILE ILE A . n 
A 1 136 GLU 136 151 151 GLU GLU A . n 
A 1 137 GLU 137 152 152 GLU GLU A . n 
A 1 138 ARG 138 153 153 ARG ARG A . n 
A 1 139 ARG 139 154 154 ARG ARG A . n 
B 2 1   GLY 1   639 ?   ?   ?   B . n 
B 2 2   PRO 2   640 ?   ?   ?   B . n 
B 2 3   TPO 3   641 641 TPO TPO B . n 
B 2 4   ILE 4   642 642 ILE ILE B . n 
B 2 5   GLU 5   643 643 GLU GLU B . n 
B 2 6   GLU 6   644 644 GLU GLU B . n 
B 2 7   VAL 7   645 645 VAL VAL B . n 
B 2 8   ASP 8   646 646 ASP ASP B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CL  1   201 1   CL  CL  A . 
D 4 HOH 1   301 196 HOH HOH A . 
D 4 HOH 2   302 225 HOH HOH A . 
D 4 HOH 3   303 226 HOH HOH A . 
D 4 HOH 4   304 185 HOH HOH A . 
D 4 HOH 5   305 34  HOH HOH A . 
D 4 HOH 6   306 169 HOH HOH A . 
D 4 HOH 7   307 218 HOH HOH A . 
D 4 HOH 8   308 4   HOH HOH A . 
D 4 HOH 9   309 168 HOH HOH A . 
D 4 HOH 10  310 176 HOH HOH A . 
D 4 HOH 11  311 2   HOH HOH A . 
D 4 HOH 12  312 6   HOH HOH A . 
D 4 HOH 13  313 164 HOH HOH A . 
D 4 HOH 14  314 48  HOH HOH A . 
D 4 HOH 15  315 114 HOH HOH A . 
D 4 HOH 16  316 35  HOH HOH A . 
D 4 HOH 17  317 180 HOH HOH A . 
D 4 HOH 18  318 197 HOH HOH A . 
D 4 HOH 19  319 158 HOH HOH A . 
D 4 HOH 20  320 25  HOH HOH A . 
D 4 HOH 21  321 77  HOH HOH A . 
D 4 HOH 22  322 108 HOH HOH A . 
D 4 HOH 23  323 84  HOH HOH A . 
D 4 HOH 24  324 109 HOH HOH A . 
D 4 HOH 25  325 16  HOH HOH A . 
D 4 HOH 26  326 228 HOH HOH A . 
D 4 HOH 27  327 78  HOH HOH A . 
D 4 HOH 28  328 216 HOH HOH A . 
D 4 HOH 29  329 1   HOH HOH A . 
D 4 HOH 30  330 160 HOH HOH A . 
D 4 HOH 31  331 56  HOH HOH A . 
D 4 HOH 32  332 12  HOH HOH A . 
D 4 HOH 33  333 31  HOH HOH A . 
D 4 HOH 34  334 120 HOH HOH A . 
D 4 HOH 35  335 115 HOH HOH A . 
D 4 HOH 36  336 55  HOH HOH A . 
D 4 HOH 37  337 33  HOH HOH A . 
D 4 HOH 38  338 136 HOH HOH A . 
D 4 HOH 39  339 81  HOH HOH A . 
D 4 HOH 40  340 179 HOH HOH A . 
D 4 HOH 41  341 94  HOH HOH A . 
D 4 HOH 42  342 170 HOH HOH A . 
D 4 HOH 43  343 51  HOH HOH A . 
D 4 HOH 44  344 36  HOH HOH A . 
D 4 HOH 45  345 26  HOH HOH A . 
D 4 HOH 46  346 104 HOH HOH A . 
D 4 HOH 47  347 23  HOH HOH A . 
D 4 HOH 48  348 93  HOH HOH A . 
D 4 HOH 49  349 18  HOH HOH A . 
D 4 HOH 50  350 50  HOH HOH A . 
D 4 HOH 51  351 163 HOH HOH A . 
D 4 HOH 52  352 157 HOH HOH A . 
D 4 HOH 53  353 3   HOH HOH A . 
D 4 HOH 54  354 153 HOH HOH A . 
D 4 HOH 55  355 215 HOH HOH A . 
D 4 HOH 56  356 229 HOH HOH A . 
D 4 HOH 57  357 80  HOH HOH A . 
D 4 HOH 58  358 60  HOH HOH A . 
D 4 HOH 59  359 40  HOH HOH A . 
D 4 HOH 60  360 165 HOH HOH A . 
D 4 HOH 61  361 200 HOH HOH A . 
D 4 HOH 62  362 39  HOH HOH A . 
D 4 HOH 63  363 227 HOH HOH A . 
D 4 HOH 64  364 11  HOH HOH A . 
D 4 HOH 65  365 182 HOH HOH A . 
D 4 HOH 66  366 9   HOH HOH A . 
D 4 HOH 67  367 181 HOH HOH A . 
D 4 HOH 68  368 205 HOH HOH A . 
D 4 HOH 69  369 135 HOH HOH A . 
D 4 HOH 70  370 90  HOH HOH A . 
D 4 HOH 71  371 219 HOH HOH A . 
D 4 HOH 72  372 106 HOH HOH A . 
D 4 HOH 73  373 49  HOH HOH A . 
D 4 HOH 74  374 73  HOH HOH A . 
D 4 HOH 75  375 206 HOH HOH A . 
D 4 HOH 76  376 22  HOH HOH A . 
D 4 HOH 77  377 202 HOH HOH A . 
D 4 HOH 78  378 154 HOH HOH A . 
D 4 HOH 79  379 76  HOH HOH A . 
D 4 HOH 80  380 188 HOH HOH A . 
D 4 HOH 81  381 8   HOH HOH A . 
D 4 HOH 82  382 186 HOH HOH A . 
D 4 HOH 83  383 58  HOH HOH A . 
D 4 HOH 84  384 171 HOH HOH A . 
D 4 HOH 85  385 174 HOH HOH A . 
D 4 HOH 86  386 175 HOH HOH A . 
D 4 HOH 87  387 91  HOH HOH A . 
D 4 HOH 88  388 142 HOH HOH A . 
D 4 HOH 89  389 177 HOH HOH A . 
D 4 HOH 90  390 92  HOH HOH A . 
D 4 HOH 91  391 210 HOH HOH A . 
D 4 HOH 92  392 59  HOH HOH A . 
D 4 HOH 93  393 156 HOH HOH A . 
D 4 HOH 94  394 88  HOH HOH A . 
D 4 HOH 95  395 141 HOH HOH A . 
D 4 HOH 96  396 217 HOH HOH A . 
D 4 HOH 97  397 82  HOH HOH A . 
D 4 HOH 98  398 74  HOH HOH A . 
D 4 HOH 99  399 143 HOH HOH A . 
D 4 HOH 100 400 138 HOH HOH A . 
D 4 HOH 101 401 198 HOH HOH A . 
D 4 HOH 102 402 220 HOH HOH A . 
D 4 HOH 103 403 37  HOH HOH A . 
D 4 HOH 104 404 189 HOH HOH A . 
D 4 HOH 105 405 38  HOH HOH A . 
D 4 HOH 106 406 96  HOH HOH A . 
D 4 HOH 107 407 223 HOH HOH A . 
D 4 HOH 108 408 184 HOH HOH A . 
D 4 HOH 109 409 167 HOH HOH A . 
D 4 HOH 110 410 113 HOH HOH A . 
D 4 HOH 111 411 20  HOH HOH A . 
D 4 HOH 112 412 97  HOH HOH A . 
D 4 HOH 113 413 149 HOH HOH A . 
D 4 HOH 114 414 24  HOH HOH A . 
D 4 HOH 115 415 212 HOH HOH A . 
D 4 HOH 116 416 199 HOH HOH A . 
D 4 HOH 117 417 224 HOH HOH A . 
D 4 HOH 118 418 140 HOH HOH A . 
D 4 HOH 119 419 190 HOH HOH A . 
D 4 HOH 120 420 119 HOH HOH A . 
D 4 HOH 121 421 161 HOH HOH A . 
D 4 HOH 122 422 193 HOH HOH A . 
D 4 HOH 123 423 72  HOH HOH A . 
D 4 HOH 124 424 123 HOH HOH A . 
D 4 HOH 125 425 162 HOH HOH A . 
D 4 HOH 126 426 230 HOH HOH A . 
D 4 HOH 127 427 214 HOH HOH A . 
D 4 HOH 128 428 52  HOH HOH A . 
D 4 HOH 129 429 159 HOH HOH A . 
D 4 HOH 130 430 102 HOH HOH A . 
D 4 HOH 131 431 203 HOH HOH A . 
D 4 HOH 132 432 187 HOH HOH A . 
D 4 HOH 133 433 204 HOH HOH A . 
D 4 HOH 134 434 30  HOH HOH A . 
D 4 HOH 135 435 201 HOH HOH A . 
D 4 HOH 136 436 152 HOH HOH A . 
D 4 HOH 137 437 195 HOH HOH A . 
E 4 HOH 1   701 98  HOH HOH B . 
E 4 HOH 2   702 221 HOH HOH B . 
E 4 HOH 3   703 166 HOH HOH B . 
E 4 HOH 4   704 178 HOH HOH B . 
E 4 HOH 5   705 100 HOH HOH B . 
E 4 HOH 6   706 222 HOH HOH B . 
E 4 HOH 7   707 101 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A SER 23  ? OG  ? A SER 8   OG  
2  1 Y 1 A GLU 77  ? CG  ? A GLU 62  CG  
3  1 Y 1 A GLU 77  ? CD  ? A GLU 62  CD  
4  1 Y 1 A GLU 77  ? OE1 ? A GLU 62  OE1 
5  1 Y 1 A GLU 77  ? OE2 ? A GLU 62  OE2 
6  1 Y 1 A ARG 128 ? CG  ? A ARG 113 CG  
7  1 Y 1 A ARG 128 ? CD  ? A ARG 113 CD  
8  1 Y 1 A ARG 128 ? NE  ? A ARG 113 NE  
9  1 Y 1 A ARG 128 ? CZ  ? A ARG 113 CZ  
10 1 Y 1 A ARG 128 ? NH1 ? A ARG 113 NH1 
11 1 Y 1 A ARG 128 ? NH2 ? A ARG 113 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21rc1_5127 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .            4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DYB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.575 
_cell.length_a_esd                 ? 
_cell.length_b                     45.932 
_cell.length_b_esd                 ? 
_cell.length_c                     78.149 
_cell.length_c_esd                 ? 
_cell.volume                       134876.961 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DYB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DYB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5, 30% (w/v) PEG 4000, 10 mM zinc chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-05-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          13.58 
_reflns.entry_id                                       9DYB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               39.6 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     34506 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.70 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.32 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.05546 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.09171 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.59 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.25 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8914 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.5321 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.612 
_reflns_shell.pdbx_CC_star                                  0.871 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.38 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.8595 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.17 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DYB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             39.60 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     18531 
_refine.ls_number_reflns_R_free                  1855 
_refine.ls_number_reflns_R_work                  16676 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.70 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1837 
_refine.ls_R_factor_R_free                       0.2203 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1797 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.8729 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1402 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        39.60 
_refine_hist.number_atoms_solvent             144 
_refine_hist.number_atoms_total               1255 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1110 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0057  ? 1144 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7822  ? 1544 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0431  ? 162  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0069  ? 207  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0050 ? 439  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.64  . . 138 1237 97.38  . . . . 0.2317 . . . . . . . . . . . 0.2690 
'X-RAY DIFFRACTION' 1.64 1.69  . . 138 1244 99.86  . . . . 0.2369 . . . . . . . . . . . 0.2787 
'X-RAY DIFFRACTION' 1.69 1.74  . . 139 1260 99.86  . . . . 0.2235 . . . . . . . . . . . 0.2851 
'X-RAY DIFFRACTION' 1.74 1.81  . . 142 1277 99.65  . . . . 0.2061 . . . . . . . . . . . 0.2502 
'X-RAY DIFFRACTION' 1.81 1.88  . . 140 1251 99.78  . . . . 0.1977 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 1.88 1.96  . . 142 1274 99.79  . . . . 0.1880 . . . . . . . . . . . 0.2575 
'X-RAY DIFFRACTION' 1.96 2.07  . . 142 1273 100.00 . . . . 0.1851 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 2.07 2.20  . . 141 1271 100.00 . . . . 0.1680 . . . . . . . . . . . 0.2251 
'X-RAY DIFFRACTION' 2.20 2.37  . . 143 1287 100.00 . . . . 0.1658 . . . . . . . . . . . 0.2071 
'X-RAY DIFFRACTION' 2.37 2.60  . . 142 1279 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2162 
'X-RAY DIFFRACTION' 2.60 2.98  . . 146 1300 100.00 . . . . 0.1824 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 2.98 3.75  . . 147 1328 100.00 . . . . 0.1645 . . . . . . . . . . . 0.2049 
'X-RAY DIFFRACTION' 3.76 39.60 . . 155 1395 99.81  . . . . 0.1624 . . . . . . . . . . . 0.1804 
# 
_struct.entry_id                     9DYB 
_struct.title                        'CHIP-TPR in complex with the phosphorylated Hsp70 tail' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DYB 
_struct_keywords.text            'ubiquitin ligase, chaperone, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CHIP_HUMAN Q9UNE7 ? 1 
;EKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHFFL
GQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERR
;
21 
2 PDB 9DYB       9DYB   ? 2 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DYB A 6 ? 139 ? Q9UNE7 21  ? 154 ? 21  154 
2 2 9DYB B 1 ? 8   ? 9DYB   639 ? 646 ? 639 646 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DYB GLY A 1 ? UNP Q9UNE7 ? ? 'expression tag' 16 1 
1 9DYB ALA A 2 ? UNP Q9UNE7 ? ? 'expression tag' 17 2 
1 9DYB MET A 3 ? UNP Q9UNE7 ? ? 'expression tag' 18 3 
1 9DYB GLY A 4 ? UNP Q9UNE7 ? ? 'expression tag' 19 4 
1 9DYB SER A 5 ? UNP Q9UNE7 ? ? 'expression tag' 20 5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1150 ? 
1 MORE         -12  ? 
1 'SSA (A^2)'  7730 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 10  ? GLY A 24  ? SER A 25  GLY A 39  1 ? 15 
HELX_P HELX_P2 AA2 LYS A 26  ? ASN A 41  ? LYS A 41  ASN A 56  1 ? 16 
HELX_P HELX_P3 AA3 VAL A 44  ? MET A 58  ? VAL A 59  MET A 73  1 ? 15 
HELX_P HELX_P4 AA4 GLN A 60  ? ASP A 75  ? GLN A 75  ASP A 90  1 ? 16 
HELX_P HELX_P5 AA5 SER A 78  ? MET A 92  ? SER A 93  MET A 107 1 ? 15 
HELX_P HELX_P6 AA6 SER A 94  ? GLN A 112 ? SER A 109 GLN A 127 1 ? 19 
HELX_P HELX_P7 AA7 ASP A 118 ? GLU A 137 ? ASP A 133 GLU A 152 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        both 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           TPO 
_struct_conn.ptnr1_label_seq_id            3 
_struct_conn.ptnr1_label_atom_id           C 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           ILE 
_struct_conn.ptnr2_label_seq_id            4 
_struct_conn.ptnr2_label_atom_id           N 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            TPO 
_struct_conn.ptnr1_auth_seq_id             641 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            ILE 
_struct_conn.ptnr2_auth_seq_id             642 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.338 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      TPO 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       3 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       TPO 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        641 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                THR 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        TPO 
_pdbx_modification_feature.type                               Phosphorylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_pdbx_entry_details.entry_id                   9DYB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 41 ? ? -102.20 77.38 
2 1 GLN A 75 ? ? -106.17 69.87 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -16.4368358194 
_pdbx_refine_tls.origin_y         -16.9316581791 
_pdbx_refine_tls.origin_z         9.65319995079 
_pdbx_refine_tls.T[1][1]          0.081270484926 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00877817994586 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.00789872026958 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0972587900148 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.00820006410689 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0804907415834 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.372290563461 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.239107413507 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.36045631004 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.1474622754 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.780584331721 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.12619690227 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          9.85614371198e-05 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0285811436183 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0158953063391 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0332015542508 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.00821281009265 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0134495454851 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0435398873839 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0238702070311 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0116876481813 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     23 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    D 
_pdbx_refine_tls_group.end_auth_seq_id     1 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 16  ? A GLY 1 
2 1 Y 1 A ALA 17  ? A ALA 2 
3 1 Y 1 A MET 18  ? A MET 3 
4 1 Y 1 A GLY 19  ? A GLY 4 
5 1 Y 1 A SER 20  ? A SER 5 
6 1 Y 1 A GLU 21  ? A GLU 6 
7 1 Y 1 A LYS 22  ? A LYS 7 
8 1 Y 1 B GLY 639 ? B GLY 1 
9 1 Y 1 B PRO 640 ? B PRO 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TPO N    N  N N 322 
TPO CA   C  N S 323 
TPO CB   C  N R 324 
TPO CG2  C  N N 325 
TPO OG1  O  N N 326 
TPO P    P  N N 327 
TPO O1P  O  N N 328 
TPO O2P  O  N N 329 
TPO O3P  O  N N 330 
TPO C    C  N N 331 
TPO O    O  N N 332 
TPO OXT  O  N N 333 
TPO H    H  N N 334 
TPO H2   H  N N 335 
TPO HA   H  N N 336 
TPO HB   H  N N 337 
TPO HG21 H  N N 338 
TPO HG22 H  N N 339 
TPO HG23 H  N N 340 
TPO HOP2 H  N N 341 
TPO HOP3 H  N N 342 
TPO HXT  H  N N 343 
TRP N    N  N N 344 
TRP CA   C  N S 345 
TRP C    C  N N 346 
TRP O    O  N N 347 
TRP CB   C  N N 348 
TRP CG   C  Y N 349 
TRP CD1  C  Y N 350 
TRP CD2  C  Y N 351 
TRP NE1  N  Y N 352 
TRP CE2  C  Y N 353 
TRP CE3  C  Y N 354 
TRP CZ2  C  Y N 355 
TRP CZ3  C  Y N 356 
TRP CH2  C  Y N 357 
TRP OXT  O  N N 358 
TRP H    H  N N 359 
TRP H2   H  N N 360 
TRP HA   H  N N 361 
TRP HB2  H  N N 362 
TRP HB3  H  N N 363 
TRP HD1  H  N N 364 
TRP HE1  H  N N 365 
TRP HE3  H  N N 366 
TRP HZ2  H  N N 367 
TRP HZ3  H  N N 368 
TRP HH2  H  N N 369 
TRP HXT  H  N N 370 
TYR N    N  N N 371 
TYR CA   C  N S 372 
TYR C    C  N N 373 
TYR O    O  N N 374 
TYR CB   C  N N 375 
TYR CG   C  Y N 376 
TYR CD1  C  Y N 377 
TYR CD2  C  Y N 378 
TYR CE1  C  Y N 379 
TYR CE2  C  Y N 380 
TYR CZ   C  Y N 381 
TYR OH   O  N N 382 
TYR OXT  O  N N 383 
TYR H    H  N N 384 
TYR H2   H  N N 385 
TYR HA   H  N N 386 
TYR HB2  H  N N 387 
TYR HB3  H  N N 388 
TYR HD1  H  N N 389 
TYR HD2  H  N N 390 
TYR HE1  H  N N 391 
TYR HE2  H  N N 392 
TYR HH   H  N N 393 
TYR HXT  H  N N 394 
VAL N    N  N N 395 
VAL CA   C  N S 396 
VAL C    C  N N 397 
VAL O    O  N N 398 
VAL CB   C  N N 399 
VAL CG1  C  N N 400 
VAL CG2  C  N N 401 
VAL OXT  O  N N 402 
VAL H    H  N N 403 
VAL H2   H  N N 404 
VAL HA   H  N N 405 
VAL HB   H  N N 406 
VAL HG11 H  N N 407 
VAL HG12 H  N N 408 
VAL HG13 H  N N 409 
VAL HG21 H  N N 410 
VAL HG22 H  N N 411 
VAL HG23 H  N N 412 
VAL HXT  H  N N 413 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TPO N   CA   sing N N 306 
TPO N   H    sing N N 307 
TPO N   H2   sing N N 308 
TPO CA  CB   sing N N 309 
TPO CA  C    sing N N 310 
TPO CA  HA   sing N N 311 
TPO CB  CG2  sing N N 312 
TPO CB  OG1  sing N N 313 
TPO CB  HB   sing N N 314 
TPO CG2 HG21 sing N N 315 
TPO CG2 HG22 sing N N 316 
TPO CG2 HG23 sing N N 317 
TPO OG1 P    sing N N 318 
TPO P   O1P  doub N N 319 
TPO P   O2P  sing N N 320 
TPO P   O3P  sing N N 321 
TPO O2P HOP2 sing N N 322 
TPO O3P HOP3 sing N N 323 
TPO C   O    doub N N 324 
TPO C   OXT  sing N N 325 
TPO OXT HXT  sing N N 326 
TRP N   CA   sing N N 327 
TRP N   H    sing N N 328 
TRP N   H2   sing N N 329 
TRP CA  C    sing N N 330 
TRP CA  CB   sing N N 331 
TRP CA  HA   sing N N 332 
TRP C   O    doub N N 333 
TRP C   OXT  sing N N 334 
TRP CB  CG   sing N N 335 
TRP CB  HB2  sing N N 336 
TRP CB  HB3  sing N N 337 
TRP CG  CD1  doub Y N 338 
TRP CG  CD2  sing Y N 339 
TRP CD1 NE1  sing Y N 340 
TRP CD1 HD1  sing N N 341 
TRP CD2 CE2  doub Y N 342 
TRP CD2 CE3  sing Y N 343 
TRP NE1 CE2  sing Y N 344 
TRP NE1 HE1  sing N N 345 
TRP CE2 CZ2  sing Y N 346 
TRP CE3 CZ3  doub Y N 347 
TRP CE3 HE3  sing N N 348 
TRP CZ2 CH2  doub Y N 349 
TRP CZ2 HZ2  sing N N 350 
TRP CZ3 CH2  sing Y N 351 
TRP CZ3 HZ3  sing N N 352 
TRP CH2 HH2  sing N N 353 
TRP OXT HXT  sing N N 354 
TYR N   CA   sing N N 355 
TYR N   H    sing N N 356 
TYR N   H2   sing N N 357 
TYR CA  C    sing N N 358 
TYR CA  CB   sing N N 359 
TYR CA  HA   sing N N 360 
TYR C   O    doub N N 361 
TYR C   OXT  sing N N 362 
TYR CB  CG   sing N N 363 
TYR CB  HB2  sing N N 364 
TYR CB  HB3  sing N N 365 
TYR CG  CD1  doub Y N 366 
TYR CG  CD2  sing Y N 367 
TYR CD1 CE1  sing Y N 368 
TYR CD1 HD1  sing N N 369 
TYR CD2 CE2  doub Y N 370 
TYR CD2 HD2  sing N N 371 
TYR CE1 CZ   doub Y N 372 
TYR CE1 HE1  sing N N 373 
TYR CE2 CZ   sing Y N 374 
TYR CE2 HE2  sing N N 375 
TYR CZ  OH   sing N N 376 
TYR OH  HH   sing N N 377 
TYR OXT HXT  sing N N 378 
VAL N   CA   sing N N 379 
VAL N   H    sing N N 380 
VAL N   H2   sing N N 381 
VAL CA  C    sing N N 382 
VAL CA  CB   sing N N 383 
VAL CA  HA   sing N N 384 
VAL C   O    doub N N 385 
VAL C   OXT  sing N N 386 
VAL CB  CG1  sing N N 387 
VAL CB  CG2  sing N N 388 
VAL CB  HB   sing N N 389 
VAL CG1 HG11 sing N N 390 
VAL CG1 HG12 sing N N 391 
VAL CG1 HG13 sing N N 392 
VAL CG2 HG21 sing N N 393 
VAL CG2 HG22 sing N N 394 
VAL CG2 HG23 sing N N 395 
VAL OXT HXT  sing N N 396 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM128595 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4KBQ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DYB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.026613 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021771 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012796 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 8   ? -2.16900  -33.93000 28.89800  1.000 44.39165 ? 23  SER A N   1 
ATOM   2    C  CA  . SER A 1 8   ? -3.05500  -32.85600 29.33800  1.000 40.77478 ? 23  SER A CA  1 
ATOM   3    C  C   . SER A 1 8   ? -2.71500  -31.54500 28.63300  1.000 37.01700 ? 23  SER A C   1 
ATOM   4    O  O   . SER A 1 8   ? -2.05700  -30.67700 29.20800  1.000 43.21755 ? 23  SER A O   1 
ATOM   5    C  CB  . SER A 1 8   ? -2.96700  -32.67500 30.85400  1.000 37.32167 ? 23  SER A CB  1 
ATOM   6    N  N   . PRO A 1 9   ? -3.16700  -31.39600 27.39100  1.000 30.89607 ? 24  PRO A N   1 
ATOM   7    C  CA  . PRO A 1 9   ? -2.77300  -30.22000 26.60500  1.000 27.79466 ? 24  PRO A CA  1 
ATOM   8    C  C   . PRO A 1 9   ? -3.44800  -28.95000 27.10100  1.000 24.03709 ? 24  PRO A C   1 
ATOM   9    O  O   . PRO A 1 9   ? -4.58900  -28.96200 27.56500  1.000 27.69714 ? 24  PRO A O   1 
ATOM   10   C  CB  . PRO A 1 9   ? -3.22900  -30.57000 25.18500  1.000 24.04448 ? 24  PRO A CB  1 
ATOM   11   C  CG  . PRO A 1 9   ? -4.35100  -31.55200 25.38800  1.000 27.28955 ? 24  PRO A CG  1 
ATOM   12   C  CD  . PRO A 1 9   ? -4.03800  -32.31600 26.63900  1.000 30.44558 ? 24  PRO A CD  1 
ATOM   13   N  N   . SER A 1 10  ? -2.72000  -27.84100 26.99300  1.000 20.61254 ? 25  SER A N   1 
ATOM   14   C  CA  . SER A 1 10  ? -3.28400  -26.53900 27.30500  1.000 19.29404 ? 25  SER A CA  1 
ATOM   15   C  C   . SER A 1 10  ? -4.25800  -26.10500 26.21200  1.000 17.43743 ? 25  SER A C   1 
ATOM   16   O  O   . SER A 1 10  ? -4.32100  -26.68700 25.12200  1.000 17.00046 ? 25  SER A O   1 
ATOM   17   C  CB  . SER A 1 10  ? -2.18000  -25.49500 27.45000  1.000 23.21262 ? 25  SER A CB  1 
ATOM   18   O  OG  . SER A 1 10  ? -1.57600  -25.22500 26.18800  1.000 19.80750 ? 25  SER A OG  1 
ATOM   19   N  N   . ALA A 1 11  ? -5.02100  -25.04700 26.51200  1.000 17.41493 ? 26  ALA A N   1 
ATOM   20   C  CA  . ALA A 1 11  ? -5.93200  -24.49000 25.51600  1.000 15.54503 ? 26  ALA A CA  1 
ATOM   21   C  C   . ALA A 1 11  ? -5.17500  -24.03200 24.27900  1.000 15.66280 ? 26  ALA A C   1 
ATOM   22   O  O   . ALA A 1 11  ? -5.61200  -24.28400 23.15100  1.000 13.60607 ? 26  ALA A O   1 
ATOM   23   C  CB  . ALA A 1 11  ? -6.73300  -23.33100 26.10800  1.000 15.46756 ? 26  ALA A CB  1 
ATOM   24   N  N   . GLN A 1 12  ? -4.02700  -23.36900 24.47100  1.000 15.42939 ? 27  GLN A N   1 
ATOM   25   C  CA  . GLN A 1 12  ? -3.23300  -22.92800 23.32500  1.000 15.78388 ? 27  GLN A CA  1 
ATOM   26   C  C   . GLN A 1 12  ? -2.71500  -24.11700 22.52400  1.000 16.53440 ? 27  GLN A C   1 
ATOM   27   O  O   . GLN A 1 12  ? -2.71700  -24.08900 21.29000  1.000 15.75591 ? 27  GLN A O   1 
ATOM   28   C  CB  . GLN A 1 12  ? -2.07100  -22.04500 23.80000  1.000 18.73502 ? 27  GLN A CB  1 
ATOM   29   C  CG  . GLN A 1 12  ? -1.01400  -21.74600 22.73500  1.000 19.81750 ? 27  GLN A CG  1 
ATOM   30   C  CD  . GLN A 1 12  ? -1.53300  -20.89800 21.57100  1.000 27.06013 ? 27  GLN A CD  1 
ATOM   31   O  OE1 . GLN A 1 12  ? -2.58800  -20.26900 21.66200  1.000 30.06106 ? 27  GLN A OE1 1 
ATOM   32   N  NE2 . GLN A 1 12  ? -0.78100  -20.88100 20.46800  1.000 27.14352 ? 27  GLN A NE2 1 
ATOM   33   N  N   . GLU A 1 13  ? -2.28000  -25.17700 23.20500  1.000 15.04537 ? 28  GLU A N   1 
ATOM   34   C  CA  . GLU A 1 13  ? -1.83400  -26.37000 22.49600  1.000 15.95551 ? 28  GLU A CA  1 
ATOM   35   C  C   . GLU A 1 13  ? -2.97200  -26.99800 21.70200  1.000 14.51508 ? 28  GLU A C   1 
ATOM   36   O  O   . GLU A 1 13  ? -2.77000  -27.48200 20.57900  1.000 14.96396 ? 28  GLU A O   1 
ATOM   37   C  CB  . GLU A 1 13  ? -1.24200  -27.37100 23.48400  1.000 16.61985 ? 28  GLU A CB  1 
ATOM   38   C  CG  . GLU A 1 13  ? 0.17800   -27.04100 23.89800  1.000 23.52699 ? 28  GLU A CG  1 
ATOM   39   C  CD  . GLU A 1 13  ? 0.69400   -27.95400 24.99400  1.000 28.48777 ? 28  GLU A CD  1 
ATOM   40   O  OE1 . GLU A 1 13  ? -0.12200  -28.42300 25.81800  1.000 29.78984 ? 28  GLU A OE1 1 
ATOM   41   O  OE2 . GLU A 1 13  ? 1.91900   -28.20600 25.03100  1.000 39.22544 ? 28  GLU A OE2 1 
ATOM   42   N  N   . LEU A 1 14  ? -4.18300  -26.98500 22.25800  1.000 12.99743 ? 29  LEU A N   1 
ATOM   43   C  CA  . LEU A 1 14  ? -5.31100  -27.55400 21.53200  1.000 10.70931 ? 29  LEU A CA  1 
ATOM   44   C  C   . LEU A 1 14  ? -5.69800  -26.68400 20.34300  1.000 11.62668 ? 29  LEU A C   1 
ATOM   45   O  O   . LEU A 1 14  ? -6.07000  -27.20700 19.28300  1.000 9.66914  ? 29  LEU A O   1 
ATOM   46   C  CB  . LEU A 1 14  ? -6.49300  -27.75200 22.47400  1.000 10.65630 ? 29  LEU A CB  1 
ATOM   47   C  CG  . LEU A 1 14  ? -6.26100  -28.92100 23.42600  1.000 12.67832 ? 29  LEU A CG  1 
ATOM   48   C  CD1 . LEU A 1 14  ? -7.24000  -28.83200 24.58500  1.000 15.14032 ? 29  LEU A CD1 1 
ATOM   49   C  CD2 . LEU A 1 14  ? -6.40100  -30.25300 22.68800  1.000 16.56040 ? 29  LEU A CD2 1 
ATOM   50   N  N   . LYS A 1 15  ? -5.61900  -25.35600 20.48300  1.000 10.94749 ? 30  LYS A N   1 
ATOM   51   C  CA  . LYS A 1 15  ? -5.85700  -24.51400 19.31300  1.000 12.24816 ? 30  LYS A CA  1 
ATOM   52   C  C   . LYS A 1 15  ? -4.83100  -24.79000 18.22100  1.000 13.06305 ? 30  LYS A C   1 
ATOM   53   O  O   . LYS A 1 15  ? -5.18000  -24.86700 17.03500  1.000 11.89634 ? 30  LYS A O   1 
ATOM   54   C  CB  . LYS A 1 15  ? -5.83100  -23.02600 19.67500  1.000 13.12775 ? 30  LYS A CB  1 
ATOM   55   C  CG  . LYS A 1 15  ? -6.32700  -22.16200 18.51200  1.000 11.56764 ? 30  LYS A CG  1 
ATOM   56   C  CD  . LYS A 1 15  ? -5.85700  -20.73500 18.60100  1.000 13.79374 ? 30  LYS A CD  1 
ATOM   57   C  CE  . LYS A 1 15  ? -4.36400  -20.65500 18.33400  1.000 17.75988 ? 30  LYS A CE  1 
ATOM   58   N  NZ  . LYS A 1 15  ? -3.91100  -19.24500 18.15500  1.000 21.81736 ? 30  LYS A NZ  1 
ATOM   59   N  N   . GLU A 1 16  ? -3.56100  -24.94500 18.60300  1.000 12.59476 ? 31  GLU A N   1 
ATOM   60   C  CA  . GLU A 1 16  ? -2.51000  -25.22800 17.62900  1.000 13.39328 ? 31  GLU A CA  1 
ATOM   61   C  C   . GLU A 1 16  ? -2.72000  -26.58100 16.95800  1.000 12.85001 ? 31  GLU A C   1 
ATOM   62   O  O   . GLU A 1 16  ? -2.48200  -26.71800 15.75200  1.000 13.14634 ? 31  GLU A O   1 
ATOM   63   C  CB  . GLU A 1 16  ? -1.14300  -25.16800 18.30800  1.000 14.39252 ? 31  GLU A CB  1 
ATOM   64   C  CG  . GLU A 1 16  ? -0.78200  -23.78900 18.84400  1.000 17.79995 ? 31  GLU A CG  1 
ATOM   65   C  CD  . GLU A 1 16  ? 0.46000   -23.80100 19.72800  1.000 18.87396 ? 31  GLU A CD  1 
ATOM   66   O  OE1 . GLU A 1 16  ? 0.88300   -24.89600 20.16100  1.000 22.79309 ? 31  GLU A OE1 1 
ATOM   67   O  OE2 . GLU A 1 16  ? 1.00600   -22.71000 19.99500  1.000 25.96233 ? 31  GLU A OE2 1 
ATOM   68   N  N   . GLN A 1 17  ? -3.16100  -27.59500 17.71600  1.000 9.75494  ? 32  GLN A N   1 
ATOM   69   C  CA  . GLN A 1 17  ? -3.49900  -28.87200 17.08800  1.000 12.19690 ? 32  GLN A CA  1 
ATOM   70   C  C   . GLN A 1 17  ? -4.66100  -28.71600 16.11400  1.000 11.93192 ? 32  GLN A C   1 
ATOM   71   O  O   . GLN A 1 17  ? -4.62600  -29.25400 15.00000  1.000 12.80247 ? 32  GLN A O   1 
ATOM   72   C  CB  . GLN A 1 17  ? -3.83600  -29.92400 18.14300  1.000 13.51994 ? 32  GLN A CB  1 
ATOM   73   C  CG  . GLN A 1 17  ? -4.20800  -31.25400 17.52500  1.000 15.73498 ? 32  GLN A CG  1 
ATOM   74   C  CD  . GLN A 1 17  ? -4.55800  -32.31300 18.56200  1.000 19.29254 ? 32  GLN A CD  1 
ATOM   75   O  OE1 . GLN A 1 17  ? -4.50400  -32.06500 19.76800  1.000 23.57733 ? 32  GLN A OE1 1 
ATOM   76   N  NE2 . GLN A 1 17  ? -4.92000  -33.49900 18.08900  1.000 24.63801 ? 32  GLN A NE2 1 
ATOM   77   N  N   . GLY A 1 18  ? -5.70100  -27.98100 16.51200  1.000 9.67215  ? 33  GLY A N   1 
ATOM   78   C  CA  . GLY A 1 18  ? -6.79500  -27.73100 15.59100  1.000 10.39675 ? 33  GLY A CA  1 
ATOM   79   C  C   . GLY A 1 18  ? -6.33100  -27.04300 14.32200  1.000 10.54695 ? 33  GLY A C   1 
ATOM   80   O  O   . GLY A 1 18  ? -6.78000  -27.38100 13.22000  1.000 10.16017 ? 33  GLY A O   1 
ATOM   81   N  N   . ASN A 1 19  ? -5.41800  -26.07500 14.45800  1.000 10.23339 ? 34  ASN A N   1 
ATOM   82   C  CA  . ASN A 1 19  ? -4.92000  -25.36500 13.28100  1.000 10.89417 ? 34  ASN A CA  1 
ATOM   83   C  C   . ASN A 1 19  ? -4.15700  -26.30500 12.35600  1.000 12.20561 ? 34  ASN A C   1 
ATOM   84   O  O   . ASN A 1 19  ? -4.25200  -26.19300 11.12500  1.000 10.81425 ? 34  ASN A O   1 
ATOM   85   C  CB  . ASN A 1 19  ? -4.02000  -24.20000 13.70100  1.000 11.02668 ? 34  ASN A CB  1 
ATOM   86   C  CG  . ASN A 1 19  ? -4.78700  -23.06500 14.36700  1.000 11.72049 ? 34  ASN A CG  1 
ATOM   87   O  OD1 . ASN A 1 19  ? -6.00800  -23.12900 14.54100  1.000 12.12143 ? 34  ASN A OD1 1 
ATOM   88   N  ND2 . ASN A 1 19  ? -4.05600  -22.02400 14.77000  1.000 13.21986 ? 34  ASN A ND2 1 
ATOM   89   N  N   . ARG A 1 20  ? -3.37400  -27.22700 12.92900  1.000 12.21234 ? 35  ARG A N   1 
ATOM   90   C  CA  . ARG A 1 20  ? -2.67200  -28.20900 12.10400  1.000 12.40707 ? 35  ARG A CA  1 
ATOM   91   C  C   . ARG A 1 20  ? -3.66700  -29.08900 11.36000  1.000 12.91784 ? 35  ARG A C   1 
ATOM   92   O  O   . ARG A 1 20  ? -3.53000  -29.31500 10.15100  1.000 11.78020 ? 35  ARG A O   1 
ATOM   93   C  CB  . ARG A 1 20  ? -1.72900  -29.06200 12.96000  1.000 13.72763 ? 35  ARG A CB  1 
ATOM   94   C  CG  . ARG A 1 20  ? -0.49700  -28.33300 13.47700  1.000 13.68210 ? 35  ARG A CG  1 
ATOM   95   C  CD  . ARG A 1 20  ? 0.53800   -29.31100 14.03400  1.000 16.11180 ? 35  ARG A CD  1 
ATOM   96   N  NE  . ARG A 1 20  ? 0.05700   -30.04200 15.19600  1.000 14.97186 ? 35  ARG A NE  1 
ATOM   97   C  CZ  . ARG A 1 20  ? 0.05300   -29.56300 16.43300  1.000 15.61388 ? 35  ARG A CZ  1 
ATOM   98   N  NH1 . ARG A 1 20  ? 0.45700   -28.33000 16.70100  1.000 16.91045 ? 35  ARG A NH1 1 
ATOM   99   N  NH2 . ARG A 1 20  ? -0.36600  -30.34100 17.42700  1.000 16.52481 ? 35  ARG A NH2 1 
ATOM   100  N  N   . LEU A 1 21  ? -4.69500  -29.57800 12.06800  1.000 13.22459 ? 36  LEU A N   1 
ATOM   101  C  CA  . LEU A 1 21  ? -5.74000  -30.35600 11.41000  1.000 11.18578 ? 36  LEU A CA  1 
ATOM   102  C  C   . LEU A 1 21  ? -6.43100  -29.53800 10.33000  1.000 11.99176 ? 36  LEU A C   1 
ATOM   103  O  O   . LEU A 1 21  ? -6.78800  -30.07100 9.27400   1.000 11.33720 ? 36  LEU A O   1 
ATOM   104  C  CB  . LEU A 1 21  ? -6.75300  -30.86000 12.44100  1.000 10.93482 ? 36  LEU A CB  1 
ATOM   105  C  CG  . LEU A 1 21  ? -6.20800  -31.95500 13.35300  1.000 11.26968 ? 36  LEU A CG  1 
ATOM   106  C  CD1 . LEU A 1 21  ? -7.06600  -32.11100 14.60100  1.000 11.73424 ? 36  LEU A CD1 1 
ATOM   107  C  CD2 . LEU A 1 21  ? -6.15900  -33.26200 12.57800  1.000 11.45291 ? 36  LEU A CD2 1 
ATOM   108  N  N   . PHE A 1 22  ? -6.61500  -28.23800 10.56900  1.000 10.00674 ? 37  PHE A N   1 
ATOM   109  C  CA  . PHE A 1 22  ? -7.20500  -27.38400 9.54500   1.000 12.05834 ? 37  PHE A CA  1 
ATOM   110  C  C   . PHE A 1 22  ? -6.32200  -27.33500 8.30100   1.000 13.82406 ? 37  PHE A C   1 
ATOM   111  O  O   . PHE A 1 22  ? -6.82100  -27.43100 7.17100   1.000 14.01998 ? 37  PHE A O   1 
ATOM   112  C  CB  . PHE A 1 22  ? -7.44200  -25.98500 10.11200  1.000 11.76939 ? 37  PHE A CB  1 
ATOM   113  C  CG  . PHE A 1 22  ? -8.27300  -25.11000 9.22000   1.000 11.75788 ? 37  PHE A CG  1 
ATOM   114  C  CD1 . PHE A 1 22  ? -9.66000  -25.11700 9.31000   1.000 13.21315 ? 37  PHE A CD1 1 
ATOM   115  C  CD2 . PHE A 1 22  ? -7.66700  -24.29400 8.27800   1.000 13.52935 ? 37  PHE A CD2 1 
ATOM   116  C  CE1 . PHE A 1 22  ? -10.43000 -24.30200 8.45300   1.000 12.63074 ? 37  PHE A CE1 1 
ATOM   117  C  CE2 . PHE A 1 22  ? -8.42100  -23.47900 7.42900   1.000 13.64641 ? 37  PHE A CE2 1 
ATOM   118  C  CZ  . PHE A 1 22  ? -9.80400  -23.49400 7.52000   1.000 14.03602 ? 37  PHE A CZ  1 
ATOM   119  N  N   . VAL A 1 23  ? -5.00300  -27.20900 8.48900   1.000 12.15194 ? 38  VAL A N   1 
ATOM   120  C  CA  . VAL A 1 23  ? -4.08700  -27.25600 7.35300   1.000 13.89431 ? 38  VAL A CA  1 
ATOM   121  C  C   . VAL A 1 23  ? -4.21900  -28.58500 6.61800   1.000 15.57885 ? 38  VAL A C   1 
ATOM   122  O  O   . VAL A 1 23  ? -4.16800  -28.63500 5.38200   1.000 15.96108 ? 38  VAL A O   1 
ATOM   123  C  CB  . VAL A 1 23  ? -2.64500  -26.99100 7.82500   1.000 15.10443 ? 38  VAL A CB  1 
ATOM   124  C  CG1 . VAL A 1 23  ? -1.65600  -27.21500 6.69000   1.000 15.67162 ? 38  VAL A CG1 1 
ATOM   125  C  CG2 . VAL A 1 23  ? -2.53600  -25.57200 8.36600   1.000 16.42524 ? 38  VAL A CG2 1 
ATOM   126  N  N   . GLY A 1 24  ? -4.40700  -29.68000 7.36100   1.000 14.02101 ? 39  GLY A N   1 
ATOM   127  C  CA  . GLY A 1 24  ? -4.62100  -30.99100 6.76500   1.000 14.27396 ? 39  GLY A CA  1 
ATOM   128  C  C   . GLY A 1 24  ? -6.00100  -31.21600 6.17300   1.000 15.13384 ? 39  GLY A C   1 
ATOM   129  O  O   . GLY A 1 24  ? -6.27900  -32.32300 5.69200   1.000 15.35890 ? 39  GLY A O   1 
ATOM   130  N  N   . ARG A 1 25  ? -6.86000  -30.19200 6.18200   1.000 14.49397 ? 40  ARG A N   1 
ATOM   131  C  CA  . ARG A 1 25  ? -8.22400  -30.27300 5.65600   1.000 14.10652 ? 40  ARG A CA  1 
ATOM   132  C  C   . ARG A 1 25  ? -9.06400  -31.30400 6.39500   1.000 13.23349 ? 40  ARG A C   1 
ATOM   133  O  O   . ARG A 1 25  ? -9.97900  -31.90600 5.82700   1.000 16.40942 ? 40  ARG A O   1 
ATOM   134  C  CB  . ARG A 1 25  ? -8.23000  -30.55400 4.14900   1.000 16.48167 ? 40  ARG A CB  1 
ATOM   135  C  CG  . ARG A 1 25  ? -7.33600  -29.62300 3.38200   1.000 17.67492 ? 40  ARG A CG  1 
ATOM   136  C  CD  . ARG A 1 25  ? -7.69800  -29.62600 1.91700   1.000 20.18861 ? 40  ARG A CD  1 
ATOM   137  N  NE  . ARG A 1 25  ? -7.57900  -30.93700 1.28800   1.000 21.48058 ? 40  ARG A NE  1 
ATOM   138  C  CZ  . ARG A 1 25  ? -6.45800  -31.42900 0.77800   1.000 21.61543 ? 40  ARG A CZ  1 
ATOM   139  N  NH1 . ARG A 1 25  ? -5.32200  -30.74800 0.81600   1.000 25.05445 ? 40  ARG A NH1 1 
ATOM   140  N  NH2 . ARG A 1 25  ? -6.47400  -32.63700 0.21400   1.000 24.02004 ? 40  ARG A NH2 1 
ATOM   141  N  N   . LYS A 1 26  ? -8.77200  -31.49600 7.68000   1.000 11.97230 ? 41  LYS A N   1 
ATOM   142  C  CA  . LYS A 1 26  ? -9.52800  -32.40600 8.53500   1.000 11.19317 ? 41  LYS A CA  1 
ATOM   143  C  C   . LYS A 1 26  ? -10.45500 -31.55200 9.39500   1.000 10.18508 ? 41  LYS A C   1 
ATOM   144  O  O   . LYS A 1 26  ? -10.21700 -31.31500 10.57800  1.000 11.10545 ? 41  LYS A O   1 
ATOM   145  C  CB  . LYS A 1 26  ? -8.56900  -33.26000 9.36700   1.000 13.60910 ? 41  LYS A CB  1 
ATOM   146  C  CG  . LYS A 1 26  ? -7.66900  -34.13200 8.48800   1.000 16.61654 ? 41  LYS A CG  1 
ATOM   147  C  CD  . LYS A 1 26  ? -6.40100  -34.58500 9.19600   1.000 20.67684 ? 41  LYS A CD  1 
ATOM   148  C  CE  . LYS A 1 26  ? -5.28100  -34.88500 8.18300   1.000 25.34806 ? 41  LYS A CE  1 
ATOM   149  N  NZ  . LYS A 1 26  ? -3.97500  -35.30500 8.81000   1.000 21.76793 ? 41  LYS A NZ  1 
ATOM   150  N  N   . TYR A 1 27  ? -11.54400 -31.09300 8.78200   1.000 9.69380  ? 42  TYR A N   1 
ATOM   151  C  CA  . TYR A 1 27  ? -12.34600 -30.03500 9.39300   1.000 10.81652 ? 42  TYR A CA  1 
ATOM   152  C  C   . TYR A 1 27  ? -13.18800 -30.51700 10.57900  1.000 8.28860  ? 42  TYR A C   1 
ATOM   153  O  O   . TYR A 1 27  ? -13.25800 -29.79800 11.58500  1.000 10.55924 ? 42  TYR A O   1 
ATOM   154  C  CB  . TYR A 1 27  ? -13.21900 -29.35300 8.32800   1.000 9.73824  ? 42  TYR A CB  1 
ATOM   155  C  CG  . TYR A 1 27  ? -12.38900 -28.77300 7.19600   1.000 11.58146 ? 42  TYR A CG  1 
ATOM   156  C  CD1 . TYR A 1 27  ? -11.37700 -27.84500 7.44600   1.000 12.33819 ? 42  TYR A CD1 1 
ATOM   157  C  CD2 . TYR A 1 27  ? -12.61400 -29.16100 5.87900   1.000 11.90542 ? 42  TYR A CD2 1 
ATOM   158  C  CE1 . TYR A 1 27  ? -10.61100 -27.31800 6.41000   1.000 12.46613 ? 42  TYR A CE1 1 
ATOM   159  C  CE2 . TYR A 1 27  ? -11.84700 -28.64400 4.83700   1.000 14.78774 ? 42  TYR A CE2 1 
ATOM   160  C  CZ  . TYR A 1 27  ? -10.85100 -27.72300 5.10800   1.000 17.43355 ? 42  TYR A CZ  1 
ATOM   161  O  OH  . TYR A 1 27  ? -10.10500 -27.21700 4.05300   1.000 16.42968 ? 42  TYR A OH  1 
ATOM   162  N  N   . PRO A 1 28  ? -13.85500 -31.68200 10.52700  1.000 11.12501 ? 43  PRO A N   1 
ATOM   163  C  CA  . PRO A 1 28  ? -14.55000 -32.14700 11.74600  1.000 11.45471 ? 43  PRO A CA  1 
ATOM   164  C  C   . PRO A 1 28  ? -13.60300 -32.37300 12.90800  1.000 10.99035 ? 43  PRO A C   1 
ATOM   165  O  O   . PRO A 1 28  ? -13.94200 -32.08700 14.06800  1.000 9.26040  ? 43  PRO A O   1 
ATOM   166  C  CB  . PRO A 1 28  ? -15.19300 -33.46300 11.29900  1.000 12.65210 ? 43  PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 28  ? -15.38700 -33.29200 9.82600   1.000 14.22621 ? 43  PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 28  ? -14.19100 -32.52600 9.36400   1.000 10.14313 ? 43  PRO A CD  1 
ATOM   169  N  N   . GLU A 1 29  ? -12.41500 -32.89500 12.61600  1.000 10.27131 ? 44  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 29  ? -11.41900 -33.10700 13.65700  1.000 9.71043  ? 44  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 29  ? -10.89700 -31.77700 14.19900  1.000 9.70172  ? 44  GLU A C   1 
ATOM   172  O  O   . GLU A 1 29  ? -10.73700 -31.61600 15.42000  1.000 9.49208  ? 44  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 29  ? -10.29000 -33.97900 13.09700  1.000 13.39398 ? 44  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 29  ? -10.69600 -35.42700 12.75600  1.000 16.63113 ? 44  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 29  ? -11.37500 -35.61400 11.38100  1.000 17.89301 ? 44  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 29  ? -11.51800 -34.65000 10.59200  1.000 15.74000 ? 44  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 29  ? -11.77700 -36.75700 11.08100  1.000 23.87788 ? 44  GLU A OE2 1 
ATOM   178  N  N   . ALA A 1 30  ? -10.65800 -30.79900 13.31900  1.000 9.91066  ? 45  ALA A N   1 
ATOM   179  C  CA  . ALA A 1 30  ? -10.22400 -29.48500 13.78900  1.000 7.87574  ? 45  ALA A CA  1 
ATOM   180  C  C   . ALA A 1 30  ? -11.29600 -28.83800 14.65600  1.000 8.74251  ? 45  ALA A C   1 
ATOM   181  O  O   . ALA A 1 30  ? -10.99400 -28.27300 15.71700  1.000 8.71432  ? 45  ALA A O   1 
ATOM   182  C  CB  . ALA A 1 30  ? -9.87100  -28.58300 12.60100  1.000 8.79002  ? 45  ALA A CB  1 
ATOM   183  N  N   . ALA A 1 31  ? -12.55400 -28.90800 14.21800  1.000 8.79061  ? 46  ALA A N   1 
ATOM   184  C  CA  . ALA A 1 31  ? -13.63700 -28.30200 14.99200  1.000 8.77778  ? 46  ALA A CA  1 
ATOM   185  C  C   . ALA A 1 31  ? -13.71500 -28.91100 16.38200  1.000 8.21255  ? 46  ALA A C   1 
ATOM   186  O  O   . ALA A 1 31  ? -13.90800 -28.19300 17.36700  1.000 8.70805  ? 46  ALA A O   1 
ATOM   187  C  CB  . ALA A 1 31  ? -14.97100 -28.47300 14.27100  1.000 8.15911  ? 46  ALA A CB  1 
ATOM   188  N  N   . ALA A 1 32  ? -13.57500 -30.23700 16.47900  1.000 9.74416  ? 47  ALA A N   1 
ATOM   189  C  CA  . ALA A 1 32  ? -13.59500 -30.87500 17.79300  1.000 8.21367  ? 47  ALA A CA  1 
ATOM   190  C  C   . ALA A 1 32  ? -12.41900 -30.42000 18.64800  1.000 9.22973  ? 47  ALA A C   1 
ATOM   191  O  O   . ALA A 1 32  ? -12.54600 -30.27500 19.87300  1.000 10.81964 ? 47  ALA A O   1 
ATOM   192  C  CB  . ALA A 1 32  ? -13.59500 -32.39500 17.64100  1.000 10.36214 ? 47  ALA A CB  1 
ATOM   193  N  N   A CYS A 1 33  ? -11.24400 -30.22200 18.03700  0.567 9.76545  ? 48  CYS A N   1 
ATOM   194  N  N   B CYS A 1 33  ? -11.26600 -30.17500 18.03000  0.433 9.07557  ? 48  CYS A N   1 
ATOM   195  C  CA  A CYS A 1 33  ? -10.11000 -29.69500 18.79000  0.567 9.71907  ? 48  CYS A CA  1 
ATOM   196  C  CA  B CYS A 1 33  ? -10.12600 -29.70400 18.80100  0.433 10.04131 ? 48  CYS A CA  1 
ATOM   197  C  C   A CYS A 1 33  ? -10.42000 -28.31600 19.35500  0.567 9.62254  ? 48  CYS A C   1 
ATOM   198  C  C   B CYS A 1 33  ? -10.36100 -28.29400 19.33100  0.433 8.96622  ? 48  CYS A C   1 
ATOM   199  O  O   A CYS A 1 33  ? -10.11900 -28.03400 20.51900  0.567 8.59608  ? 48  CYS A O   1 
ATOM   200  O  O   B CYS A 1 33  ? -9.95000  -27.97100 20.45000  0.433 8.48475  ? 48  CYS A O   1 
ATOM   201  C  CB  A CYS A 1 33  ? -8.86100  -29.62600 17.90800  0.567 10.65591 ? 48  CYS A CB  1 
ATOM   202  C  CB  B CYS A 1 33  ? -8.86400  -29.75800 17.95100  0.433 10.55824 ? 48  CYS A CB  1 
ATOM   203  S  SG  A CYS A 1 33  ? -7.88300  -31.14100 17.81000  0.567 11.98441 ? 48  CYS A SG  1 
ATOM   204  S  SG  B CYS A 1 33  ? -7.42100  -30.08800 18.93200  0.433 13.05774 ? 48  CYS A SG  1 
ATOM   205  N  N   . TYR A 1 34  ? -11.02000 -27.43800 18.54200  1.000 9.53379  ? 49  TYR A N   1 
ATOM   206  C  CA  . TYR A 1 34  ? -11.36800 -26.10900 19.04600  1.000 8.13715  ? 49  TYR A CA  1 
ATOM   207  C  C   . TYR A 1 34  ? -12.37500 -26.21400 20.18400  1.000 8.07262  ? 49  TYR A C   1 
ATOM   208  O  O   . TYR A 1 34  ? -12.32000 -25.43200 21.13800  1.000 8.84743  ? 49  TYR A O   1 
ATOM   209  C  CB  . TYR A 1 34  ? -11.89600 -25.22300 17.91300  1.000 8.42247  ? 49  TYR A CB  1 
ATOM   210  C  CG  . TYR A 1 34  ? -10.87400 -24.99100 16.81500  1.000 7.85224  ? 49  TYR A CG  1 
ATOM   211  C  CD1 . TYR A 1 34  ? -9.56900  -24.60300 17.12000  1.000 8.52058  ? 49  TYR A CD1 1 
ATOM   212  C  CD2 . TYR A 1 34  ? -11.21400 -25.18200 15.48400  1.000 8.21980  ? 49  TYR A CD2 1 
ATOM   213  C  CE1 . TYR A 1 34  ? -8.62700  -24.39400 16.11600  1.000 8.99548  ? 49  TYR A CE1 1 
ATOM   214  C  CE2 . TYR A 1 34  ? -10.29500 -24.97600 14.47700  1.000 9.30941  ? 49  TYR A CE2 1 
ATOM   215  C  CZ  . TYR A 1 34  ? -9.00900  -24.59000 14.79600  1.000 8.89530  ? 49  TYR A CZ  1 
ATOM   216  O  OH  . TYR A 1 34  ? -8.10400  -24.40700 13.79100  1.000 9.29657  ? 49  TYR A OH  1 
ATOM   217  N  N   . GLY A 1 35  ? -13.26700 -27.20200 20.12400  1.000 9.03189  ? 50  GLY A N   1 
ATOM   218  C  CA  . GLY A 1 35  ? -14.17000 -27.43200 21.23900  1.000 7.89077  ? 50  GLY A CA  1 
ATOM   219  C  C   . GLY A 1 35  ? -13.42800 -27.77600 22.51400  1.000 8.94593  ? 50  GLY A C   1 
ATOM   220  O  O   . GLY A 1 35  ? -13.81100 -27.34100 23.60800  1.000 8.09109  ? 50  GLY A O   1 
ATOM   221  N  N   . ARG A 1 36  ? -12.36100 -28.57300 22.39300  1.000 9.10500  ? 51  ARG A N   1 
ATOM   222  C  CA  . ARG A 1 36  ? -11.54800 -28.89500 23.56200  1.000 8.79218  ? 51  ARG A CA  1 
ATOM   223  C  C   . ARG A 1 36  ? -10.85000 -27.65000 24.08500  1.000 10.42916 ? 51  ARG A C   1 
ATOM   224  O  O   . ARG A 1 36  ? -10.71900 -27.46500 25.30500  1.000 10.15930 ? 51  ARG A O   1 
ATOM   225  C  CB  . ARG A 1 36  ? -10.51400 -29.98100 23.22400  1.000 11.16009 ? 51  ARG A CB  1 
ATOM   226  C  CG  . ARG A 1 36  ? -11.10500 -31.34500 22.89900  1.000 12.88927 ? 51  ARG A CG  1 
ATOM   227  C  CD  . ARG A 1 36  ? -10.02500 -32.39800 22.66800  1.000 12.80197 ? 51  ARG A CD  1 
ATOM   228  N  NE  . ARG A 1 36  ? -9.23900  -32.66000 23.86400  1.000 18.82771 ? 51  ARG A NE  1 
ATOM   229  C  CZ  . ARG A 1 36  ? -8.09100  -33.32300 23.86300  1.000 19.07825 ? 51  ARG A CZ  1 
ATOM   230  N  NH1 . ARG A 1 36  ? -7.54200  -33.74700 22.73700  1.000 24.05059 ? 51  ARG A NH1 1 
ATOM   231  N  NH2 . ARG A 1 36  ? -7.48100  -33.56700 25.02000  1.000 20.52750 ? 51  ARG A NH2 1 
ATOM   232  N  N   . ALA A 1 37  ? -10.38800 -26.78500 23.17800  1.000 8.14499  ? 52  ALA A N   1 
ATOM   233  C  CA  . ALA A 1 37  ? -9.76200  -25.54200 23.61600  1.000 9.60431  ? 52  ALA A CA  1 
ATOM   234  C  C   . ALA A 1 37  ? -10.76000 -24.67400 24.36400  1.000 10.60823 ? 52  ALA A C   1 
ATOM   235  O  O   . ALA A 1 37  ? -10.42300 -24.07500 25.39700  1.000 9.50702  ? 52  ALA A O   1 
ATOM   236  C  CB  . ALA A 1 37  ? -9.17400  -24.80000 22.41900  1.000 9.58306  ? 52  ALA A CB  1 
ATOM   237  N  N   . ILE A 1 38  ? -12.00500 -24.62900 23.87400  1.000 8.62509  ? 53  ILE A N   1 
ATOM   238  C  CA  . ILE A 1 38  ? -13.07100 -23.88000 24.53000  1.000 9.39243  ? 53  ILE A CA  1 
ATOM   239  C  C   . ILE A 1 38  ? -13.31900 -24.42100 25.93300  1.000 10.28417 ? 53  ILE A C   1 
ATOM   240  O  O   . ILE A 1 38  ? -13.52100 -23.65800 26.88800  1.000 10.61424 ? 53  ILE A O   1 
ATOM   241  C  CB  . ILE A 1 38  ? -14.33600 -23.92300 23.65300  1.000 10.04469 ? 53  ILE A CB  1 
ATOM   242  C  CG1 . ILE A 1 38  ? -14.09700 -23.10500 22.37400  1.000 10.54373 ? 53  ILE A CG1 1 
ATOM   243  C  CG2 . ILE A 1 38  ? -15.58200 -23.45500 24.43100  1.000 9.70659  ? 53  ILE A CG2 1 
ATOM   244  C  CD1 . ILE A 1 38  ? -15.12400 -23.36100 21.26600  1.000 9.84493  ? 53  ILE A CD1 1 
ATOM   245  N  N   . THR A 1 39  ? -13.27900 -25.74700 26.08900  1.000 9.29221  ? 54  THR A N   1 
ATOM   246  C  CA  . THR A 1 39  ? -13.43600 -26.33100 27.41700  1.000 9.08480  ? 54  THR A CA  1 
ATOM   247  C  C   . THR A 1 39  ? -12.38600 -25.79900 28.38600  1.000 12.32741 ? 54  THR A C   1 
ATOM   248  O  O   . THR A 1 39  ? -12.68900 -25.51200 29.55200  1.000 13.19636 ? 54  THR A O   1 
ATOM   249  C  CB  . THR A 1 39  ? -13.35300 -27.85700 27.31700  1.000 11.95574 ? 54  THR A CB  1 
ATOM   250  O  OG1 . THR A 1 39  ? -14.48400 -28.35800 26.58900  1.000 11.43310 ? 54  THR A OG1 1 
ATOM   251  C  CG2 . THR A 1 39  ? -13.35000 -28.47300 28.66200  1.000 11.92706 ? 54  THR A CG2 1 
ATOM   252  N  N   . ARG A 1 40  ? -11.14700 -25.63800 27.92000  1.000 10.86075 ? 55  ARG A N   1 
ATOM   253  C  CA  . ARG A 1 40  ? -10.10200 -25.17700 28.81900  1.000 10.97029 ? 55  ARG A CA  1 
ATOM   254  C  C   . ARG A 1 40  ? -10.12600 -23.67100 29.03000  1.000 13.38863 ? 55  ARG A C   1 
ATOM   255  O  O   . ARG A 1 40  ? -9.75300  -23.20300 30.10900  1.000 15.04165 ? 55  ARG A O   1 
ATOM   256  C  CB  . ARG A 1 40  ? -8.73800  -25.62400 28.30300  1.000 13.71632 ? 55  ARG A CB  1 
ATOM   257  C  CG  . ARG A 1 40  ? -8.43200  -27.01700 28.78300  1.000 22.69797 ? 55  ARG A CG  1 
ATOM   258  C  CD  . ARG A 1 40  ? -7.95200  -27.86800 27.67300  1.000 26.17532 ? 55  ARG A CD  1 
ATOM   259  N  NE  . ARG A 1 40  ? -7.79500  -29.26200 28.07200  1.000 29.31663 ? 55  ARG A NE  1 
ATOM   260  C  CZ  . ARG A 1 40  ? -8.64100  -30.23500 27.75500  1.000 31.09874 ? 55  ARG A CZ  1 
ATOM   261  N  NH1 . ARG A 1 40  ? -9.77100  -29.99000 27.10300  1.000 25.23282 ? 55  ARG A NH1 1 
ATOM   262  N  NH2 . ARG A 1 40  ? -8.33900  -31.48800 28.08600  1.000 32.95257 ? 55  ARG A NH2 1 
ATOM   263  N  N   . ASN A 1 41  ? -10.55000 -22.90100 28.03900  1.000 11.80508 ? 56  ASN A N   1 
ATOM   264  C  CA  . ASN A 1 41  ? -10.70100 -21.45500 28.20400  1.000 11.39828 ? 56  ASN A CA  1 
ATOM   265  C  C   . ASN A 1 41  ? -11.81000 -21.01200 27.26500  1.000 10.19425 ? 56  ASN A C   1 
ATOM   266  O  O   . ASN A 1 41  ? -11.58200 -20.81200 26.06200  1.000 10.46820 ? 56  ASN A O   1 
ATOM   267  C  CB  . ASN A 1 41  ? -9.40400  -20.70900 27.91100  1.000 14.56744 ? 56  ASN A CB  1 
ATOM   268  C  CG  . ASN A 1 41  ? -9.51300  -19.22200 28.17500  1.000 13.85404 ? 56  ASN A CG  1 
ATOM   269  O  OD1 . ASN A 1 41  ? -10.59100 -18.69700 28.45000  1.000 14.39504 ? 56  ASN A OD1 1 
ATOM   270  N  ND2 . ASN A 1 41  ? -8.38400  -18.53000 28.09200  1.000 17.68630 ? 56  ASN A ND2 1 
ATOM   271  N  N   . PRO A 1 42  ? -13.03400 -20.85400 27.77300  1.000 10.32933 ? 57  PRO A N   1 
ATOM   272  C  CA  . PRO A 1 42  ? -14.15400 -20.48000 26.90400  1.000 11.70339 ? 57  PRO A CA  1 
ATOM   273  C  C   . PRO A 1 42  ? -14.26500 -18.99000 26.64200  1.000 10.60619 ? 57  PRO A C   1 
ATOM   274  O  O   . PRO A 1 42  ? -15.25400 -18.55500 26.04300  1.000 12.46638 ? 57  PRO A O   1 
ATOM   275  C  CB  . PRO A 1 42  ? -15.36800 -20.99500 27.69700  1.000 11.63640 ? 57  PRO A CB  1 
ATOM   276  C  CG  . PRO A 1 42  ? -14.94500 -20.82900 29.12400  1.000 12.74889 ? 57  PRO A CG  1 
ATOM   277  C  CD  . PRO A 1 42  ? -13.46600 -21.13300 29.15700  1.000 15.06700 ? 57  PRO A CD  1 
ATOM   278  N  N   . LEU A 1 43  ? -13.26900 -18.20300 27.05800  1.000 11.71271 ? 58  LEU A N   1 
ATOM   279  C  CA  . LEU A 1 43  ? -13.32700 -16.75300 26.94100  1.000 11.49811 ? 58  LEU A CA  1 
ATOM   280  C  C   . LEU A 1 43  ? -12.49100 -16.20800 25.78300  1.000 13.00686 ? 58  LEU A C   1 
ATOM   281  O  O   . LEU A 1 43  ? -12.21800 -14.99900 25.74500  1.000 14.52329 ? 58  LEU A O   1 
ATOM   282  C  CB  . LEU A 1 43  ? -12.88000 -16.11700 28.25700  1.000 12.41410 ? 58  LEU A CB  1 
ATOM   283  C  CG  . LEU A 1 43  ? -13.60400 -16.68900 29.47000  1.000 15.09975 ? 58  LEU A CG  1 
ATOM   284  C  CD1 . LEU A 1 43  ? -13.03900 -16.08500 30.76100  1.000 18.43124 ? 58  LEU A CD1 1 
ATOM   285  C  CD2 . LEU A 1 43  ? -15.10500 -16.44300 29.34600  1.000 16.96296 ? 58  LEU A CD2 1 
ATOM   286  N  N   . VAL A 1 44  ? -12.09400 -17.06000 24.84000  1.000 11.23675 ? 59  VAL A N   1 
ATOM   287  C  CA  . VAL A 1 44  ? -11.20800 -16.68300 23.73900  1.000 12.04028 ? 59  VAL A CA  1 
ATOM   288  C  C   . VAL A 1 44  ? -12.01700 -16.72000 22.44900  1.000 12.27510 ? 59  VAL A C   1 
ATOM   289  O  O   . VAL A 1 44  ? -12.38100 -17.79600 21.96300  1.000 11.27875 ? 59  VAL A O   1 
ATOM   290  C  CB  . VAL A 1 44  ? -9.98700  -17.60600 23.65200  1.000 12.55341 ? 59  VAL A CB  1 
ATOM   291  C  CG1 . VAL A 1 44  ? -9.04900  -17.16100 22.52300  1.000 15.30506 ? 59  VAL A CG1 1 
ATOM   292  C  CG2 . VAL A 1 44  ? -9.25200  -17.65400 25.00000  1.000 13.18252 ? 59  VAL A CG2 1 
ATOM   293  N  N   . ALA A 1 45  ? -12.28600 -15.53700 21.88800  1.000 12.30656 ? 60  ALA A N   1 
ATOM   294  C  CA  . ALA A 1 45  ? -13.18800 -15.43900 20.74500  1.000 9.85725  ? 60  ALA A CA  1 
ATOM   295  C  C   . ALA A 1 45  ? -12.64800 -16.19800 19.53300  1.000 10.29580 ? 60  ALA A C   1 
ATOM   296  O  O   . ALA A 1 45  ? -13.42100 -16.77700 18.75900  1.000 11.21959 ? 60  ALA A O   1 
ATOM   297  C  CB  . ALA A 1 45  ? -13.42300 -13.96600 20.39700  1.000 11.45328 ? 60  ALA A CB  1 
ATOM   298  N  N   . VAL A 1 46  ? -11.32100 -16.21000 19.36000  1.000 11.34122 ? 61  VAL A N   1 
ATOM   299  C  CA  . VAL A 1 46  ? -10.70000 -16.84900 18.19900  1.000 11.34626 ? 61  VAL A CA  1 
ATOM   300  C  C   . VAL A 1 46  ? -10.99200 -18.34600 18.14300  1.000 9.07062  ? 61  VAL A C   1 
ATOM   301  O  O   . VAL A 1 46  ? -11.08200 -18.91900 17.04800  1.000 10.42314 ? 61  VAL A O   1 
ATOM   302  C  CB  . VAL A 1 46  ? -9.18300  -16.54800 18.20000  1.000 10.82775 ? 61  VAL A CB  1 
ATOM   303  C  CG1 . VAL A 1 46  ? -8.37700  -17.67100 17.56200  1.000 17.69201 ? 61  VAL A CG1 1 
ATOM   304  C  CG2 . VAL A 1 46  ? -8.92800  -15.23100 17.48700  1.000 15.30349 ? 61  VAL A CG2 1 
ATOM   305  N  N   . TYR A 1 47  ? -11.17700 -19.00700 19.29400  1.000 11.80808 ? 62  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 47  ? -11.54800 -20.42500 19.24500  1.000 9.75064  ? 62  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 47  ? -12.88000 -20.61500 18.53200  1.000 8.76468  ? 62  TYR A C   1 
ATOM   308  O  O   . TYR A 1 47  ? -13.06400 -21.58900 17.78600  1.000 8.24356  ? 62  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 47  ? -11.63200 -21.03800 20.65000  1.000 9.92583  ? 62  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 47  ? -10.37900 -20.97200 21.48300  1.000 11.18425 ? 62  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 47  ? -9.15200  -20.63300 20.93000  1.000 12.73621 ? 62  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 47  ? -10.42600 -21.24600 22.85100  1.000 11.20386 ? 62  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 47  ? -8.01300  -20.55700 21.71900  1.000 12.14295 ? 62  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 47  ? -9.29500  -21.18200 23.64100  1.000 11.80892 ? 62  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 47  ? -8.08900  -20.84000 23.07200  1.000 13.83797 ? 62  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 47  ? -6.96400  -20.77000 23.86800  1.000 14.35810 ? 62  TYR A OH  1 
ATOM   317  N  N   . TYR A 1 48  ? -13.82500 -19.69000 18.76000  1.000 8.52764  ? 63  TYR A N   1 
ATOM   318  C  CA  . TYR A 1 48  ? -15.15100 -19.76800 18.16300  1.000 10.10101 ? 63  TYR A CA  1 
ATOM   319  C  C   . TYR A 1 48  ? -15.13700 -19.39700 16.68900  1.000 9.35727  ? 63  TYR A C   1 
ATOM   320  O  O   . TYR A 1 48  ? -15.82100 -20.04800 15.89200  1.000 9.38155  ? 63  TYR A O   1 
ATOM   321  C  CB  . TYR A 1 48  ? -16.12400 -18.86700 18.91600  1.000 9.82667  ? 63  TYR A CB  1 
ATOM   322  C  CG  . TYR A 1 48  ? -16.33400 -19.26700 20.35900  1.000 9.85081  ? 63  TYR A CG  1 
ATOM   323  C  CD1 . TYR A 1 48  ? -17.21900 -20.27800 20.70300  1.000 11.59989 ? 63  TYR A CD1 1 
ATOM   324  C  CD2 . TYR A 1 48  ? -15.64300 -18.62300 21.37600  1.000 11.47020 ? 63  TYR A CD2 1 
ATOM   325  C  CE1 . TYR A 1 48  ? -17.40900 -20.63700 22.03400  1.000 11.96557 ? 63  TYR A CE1 1 
ATOM   326  C  CE2 . TYR A 1 48  ? -15.82500 -18.96800 22.69700  1.000 12.47285 ? 63  TYR A CE2 1 
ATOM   327  C  CZ  . TYR A 1 48  ? -16.70100 -19.97000 23.02400  1.000 12.88056 ? 63  TYR A CZ  1 
ATOM   328  O  OH  . TYR A 1 48  ? -16.86100 -20.28300 24.35100  1.000 13.99735 ? 63  TYR A OH  1 
ATOM   329  N  N   . THR A 1 49  ? -14.40400 -18.34500 16.30100  1.000 9.26195  ? 64  THR A N   1 
ATOM   330  C  CA  . THR A 1 49  ? -14.34300 -18.04600 14.87200  1.000 9.90204  ? 64  THR A CA  1 
ATOM   331  C  C   . THR A 1 49  ? -13.55600 -19.10500 14.11700  1.000 9.46472  ? 64  THR A C   1 
ATOM   332  O  O   . THR A 1 49  ? -13.88800 -19.40800 12.96300  1.000 8.75387  ? 64  THR A O   1 
ATOM   333  C  CB  . THR A 1 49  ? -13.77700 -16.64300 14.59900  1.000 10.83832 ? 64  THR A CB  1 
ATOM   334  O  OG1 . THR A 1 49  ? -12.54700 -16.43000 15.30300  1.000 11.25765 ? 64  THR A OG1 1 
ATOM   335  C  CG2 . THR A 1 49  ? -14.78100 -15.57700 15.02000  1.000 13.30050 ? 64  THR A CG2 1 
ATOM   336  N  N   . ASN A 1 50  ? -12.52700 -19.69600 14.74400  1.000 7.68841  ? 65  ASN A N   1 
ATOM   337  C  CA  . ASN A 1 50  ? -11.84500 -20.81400 14.09700  1.000 8.28479  ? 65  ASN A CA  1 
ATOM   338  C  C   . ASN A 1 50  ? -12.81500 -21.96200 13.86200  1.000 9.41906  ? 65  ASN A C   1 
ATOM   339  O  O   . ASN A 1 50  ? -12.85000 -22.54800 12.77000  1.000 8.24349  ? 65  ASN A O   1 
ATOM   340  C  CB  . ASN A 1 50  ? -10.66600 -21.30000 14.94200  1.000 8.14744  ? 65  ASN A CB  1 
ATOM   341  C  CG  . ASN A 1 50  ? -9.41000  -20.46400 14.77400  1.000 12.00018 ? 65  ASN A CG  1 
ATOM   342  O  OD1 . ASN A 1 50  ? -9.39800  -19.41800 14.10600  1.000 10.35866 ? 65  ASN A OD1 1 
ATOM   343  N  ND2 . ASN A 1 50  ? -8.33200  -20.91900 15.41500  1.000 11.20007 ? 65  ASN A ND2 1 
ATOM   344  N  N   . ARG A 1 51  ? -13.61200 -22.30400 14.88400  1.000 7.17134  ? 66  ARG A N   1 
ATOM   345  C  CA  . ARG A 1 51  ? -14.55200 -23.41100 14.72000  1.000 6.60944  ? 66  ARG A CA  1 
ATOM   346  C  C   . ARG A 1 51  ? -15.64200 -23.04600 13.71300  1.000 8.78425  ? 66  ARG A C   1 
ATOM   347  O  O   . ARG A 1 51  ? -16.06800 -23.89300 12.91800  1.000 9.30845  ? 66  ARG A O   1 
ATOM   348  C  CB  . ARG A 1 51  ? -15.15200 -23.82200 16.07200  1.000 8.19052  ? 66  ARG A CB  1 
ATOM   349  C  CG  . ARG A 1 51  ? -15.86800 -25.17600 15.98000  1.000 8.99614  ? 66  ARG A CG  1 
ATOM   350  C  CD  . ARG A 1 51  ? -16.21200 -25.71800 17.33500  1.000 9.79504  ? 66  ARG A CD  1 
ATOM   351  N  NE  . ARG A 1 51  ? -17.19200 -24.87400 18.00600  1.000 8.97404  ? 66  ARG A NE  1 
ATOM   352  C  CZ  . ARG A 1 51  ? -17.73100 -25.17500 19.17500  1.000 10.94270 ? 66  ARG A CZ  1 
ATOM   353  N  NH1 . ARG A 1 51  ? -17.42500 -26.30500 19.80500  1.000 11.44370 ? 66  ARG A NH1 1 
ATOM   354  N  NH2 . ARG A 1 51  ? -18.58400 -24.31700 19.74000  1.000 10.97107 ? 66  ARG A NH2 1 
ATOM   355  N  N   . ALA A 1 52  ? -16.08000 -21.78500 13.71100  1.000 10.09149 ? 67  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 52  ? -17.08500 -21.35300 12.74800  1.000 8.55871  ? 67  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 52  ? -16.60600 -21.57300 11.32000  1.000 9.64082  ? 67  ALA A C   1 
ATOM   358  O  O   . ALA A 1 52  ? -17.38200 -22.00400 10.45800  1.000 9.27654  ? 67  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 52  ? -17.43000 -19.87900 12.96900  1.000 9.62608  ? 67  ALA A CB  1 
ATOM   360  N  N   . LEU A 1 53  ? -15.33000 -21.27300 11.04900  1.000 8.01832  ? 68  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 53  ? -14.78300 -21.51100 9.71500   1.000 7.89470  ? 68  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 53  ? -14.79900 -22.99800 9.36500   1.000 10.02076 ? 68  LEU A C   1 
ATOM   363  O  O   . LEU A 1 53  ? -15.10000 -23.37000 8.22200   1.000 9.25087  ? 68  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 53  ? -13.36200 -20.94900 9.62900   1.000 9.83684  ? 68  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 53  ? -12.60400 -21.12000 8.31100   1.000 10.49450 ? 68  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 53  ? -13.41800 -20.57700 7.13900   1.000 12.05321 ? 68  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 53  ? -11.26700 -20.41000 8.41700   1.000 10.21043 ? 68  LEU A CD2 1 
ATOM   368  N  N   . CYS A 1 54  ? -14.50000 -23.86600 10.33800  1.000 8.45627  ? 69  CYS A N   1 
ATOM   369  C  CA  . CYS A 1 54  ? -14.59900 -25.30800 10.09800  1.000 9.27013  ? 69  CYS A CA  1 
ATOM   370  C  C   . CYS A 1 54  ? -16.01900 -25.69400 9.72500   1.000 9.24645  ? 69  CYS A C   1 
ATOM   371  O  O   . CYS A 1 54  ? -16.24600 -26.43300 8.75800   1.000 9.20103  ? 69  CYS A O   1 
ATOM   372  C  CB  . CYS A 1 54  ? -14.17200 -26.09200 11.34200  1.000 8.16427  ? 69  CYS A CB  1 
ATOM   373  S  SG  . CYS A 1 54  ? -12.42600 -25.96700 11.74800  1.000 11.62853 ? 69  CYS A SG  1 
ATOM   374  N  N   . TYR A 1 55  ? -16.99400 -25.20800 10.49700  1.000 8.30500  ? 70  TYR A N   1 
ATOM   375  C  CA  . TYR A 1 55  ? -18.38600 -25.52200 10.20600  1.000 9.44482  ? 70  TYR A CA  1 
ATOM   376  C  C   . TYR A 1 55  ? -18.79400 -25.01200 8.82500   1.000 9.52360  ? 70  TYR A C   1 
ATOM   377  O  O   . TYR A 1 55  ? -19.55900 -25.67400 8.11900   1.000 9.38990  ? 70  TYR A O   1 
ATOM   378  C  CB  . TYR A 1 55  ? -19.29900 -24.94500 11.29200  1.000 9.76371  ? 70  TYR A CB  1 
ATOM   379  C  CG  . TYR A 1 55  ? -19.21000 -25.67600 12.61700  1.000 11.13000 ? 70  TYR A CG  1 
ATOM   380  C  CD1 . TYR A 1 55  ? -19.10800 -27.06200 12.66700  1.000 11.75540 ? 70  TYR A CD1 1 
ATOM   381  C  CD2 . TYR A 1 55  ? -19.23700 -24.97800 13.82300  1.000 10.90523 ? 70  TYR A CD2 1 
ATOM   382  C  CE1 . TYR A 1 55  ? -19.03600 -27.73800 13.88700  1.000 14.29891 ? 70  TYR A CE1 1 
ATOM   383  C  CE2 . TYR A 1 55  ? -19.16600 -25.64600 15.04300  1.000 10.38950 ? 70  TYR A CE2 1 
ATOM   384  C  CZ  . TYR A 1 55  ? -19.06000 -27.01400 15.07000  1.000 13.29110 ? 70  TYR A CZ  1 
ATOM   385  O  OH  . TYR A 1 55  ? -18.99100 -27.67500 16.27500  1.000 12.41741 ? 70  TYR A OH  1 
ATOM   386  N  N   . LEU A 1 56  ? -18.30600 -23.82900 8.42100   1.000 8.45355  ? 71  LEU A N   1 
ATOM   387  C  CA  . LEU A 1 56  ? -18.58700 -23.35700 7.06700   1.000 10.69299 ? 71  LEU A CA  1 
ATOM   388  C  C   . LEU A 1 56  ? -18.03600 -24.32800 6.03000   1.000 11.99152 ? 71  LEU A C   1 
ATOM   389  O  O   . LEU A 1 56  ? -18.71100 -24.64700 5.04200   1.000 12.51235 ? 71  LEU A O   1 
ATOM   390  C  CB  . LEU A 1 56  ? -18.00300 -21.95700 6.84700   1.000 11.62946 ? 71  LEU A CB  1 
ATOM   391  C  CG  . LEU A 1 56  ? -18.78400 -20.80300 7.48100   1.000 13.61728 ? 71  LEU A CG  1 
ATOM   392  C  CD1 . LEU A 1 56  ? -17.99700 -19.50400 7.39500   1.000 13.40941 ? 71  LEU A CD1 1 
ATOM   393  C  CD2 . LEU A 1 56  ? -20.11900 -20.66500 6.76200   1.000 17.60650 ? 71  LEU A CD2 1 
ATOM   394  N  N   . LYS A 1 57  ? -16.80400 -24.80700 6.23200   1.000 11.31507 ? 72  LYS A N   1 
ATOM   395  C  CA  . LYS A 1 57  ? -16.22900 -25.77000 5.29600   1.000 11.72369 ? 72  LYS A CA  1 
ATOM   396  C  C   . LYS A 1 57  ? -17.03900 -27.05800 5.26500   1.000 11.64773 ? 72  LYS A C   1 
ATOM   397  O  O   . LYS A 1 57  ? -17.08600 -27.74400 4.23700   1.000 12.71876 ? 72  LYS A O   1 
ATOM   398  C  CB  . LYS A 1 57  ? -14.77600 -26.08000 5.66900   1.000 14.46697 ? 72  LYS A CB  1 
ATOM   399  C  CG  . LYS A 1 57  ? -13.82000 -24.91400 5.58100   1.000 16.35962 ? 72  LYS A CG  1 
ATOM   400  C  CD  . LYS A 1 57  ? -13.39200 -24.66500 4.15900   1.000 22.78964 ? 72  LYS A CD  1 
ATOM   401  C  CE  . LYS A 1 57  ? -12.36900 -23.55000 4.09000   1.000 28.97935 ? 72  LYS A CE  1 
ATOM   402  N  NZ  . LYS A 1 57  ? -11.83900 -23.41600 2.70400   1.000 34.15834 ? 72  LYS A NZ  1 
ATOM   403  N  N   . MET A 1 58  ? -17.65700 -27.41200 6.39300   1.000 11.21212 ? 73  MET A N   1 
ATOM   404  C  CA  . MET A 1 58  ? -18.47600 -28.60700 6.52100   1.000 12.10038 ? 73  MET A CA  1 
ATOM   405  C  C   . MET A 1 58  ? -19.92900 -28.37400 6.10200   1.000 13.32632 ? 73  MET A C   1 
ATOM   406  O  O   . MET A 1 58  ? -20.75100 -29.29000 6.24500   1.000 13.54039 ? 73  MET A O   1 
ATOM   407  C  CB  . MET A 1 58  ? -18.42300 -29.12200 7.97800   1.000 10.78946 ? 73  MET A CB  1 
ATOM   408  C  CG  . MET A 1 58  ? -17.02300 -29.55700 8.46400   1.000 13.71292 ? 73  MET A CG  1 
ATOM   409  S  SD  . MET A 1 58  ? -16.80300 -29.48000 10.27600  1.000 13.80770 ? 73  MET A SD  1 
ATOM   410  C  CE  . MET A 1 58  ? -18.08500 -30.61300 10.83300  1.000 19.14334 ? 73  MET A CE  1 
ATOM   411  N  N   . GLN A 1 59  ? -20.26200 -27.17800 5.59300   1.000 12.07598 ? 74  GLN A N   1 
ATOM   412  C  CA  . GLN A 1 59  ? -21.62100 -26.81400 5.17400   1.000 13.90828 ? 74  GLN A CA  1 
ATOM   413  C  C   . GLN A 1 59  ? -22.60400 -26.84400 6.34000   1.000 15.70425 ? 74  GLN A C   1 
ATOM   414  O  O   . GLN A 1 59  ? -23.80000 -27.08100 6.15800   1.000 15.85072 ? 74  GLN A O   1 
ATOM   415  C  CB  . GLN A 1 59  ? -22.12100 -27.71100 4.03900   1.000 19.22731 ? 74  GLN A CB  1 
ATOM   416  C  CG  . GLN A 1 59  ? -21.06200 -28.04500 3.01600   1.000 24.07362 ? 74  GLN A CG  1 
ATOM   417  C  CD  . GLN A 1 59  ? -21.05600 -27.10100 1.85000   1.000 28.86474 ? 74  GLN A CD  1 
ATOM   418  O  OE1 . GLN A 1 59  ? -21.22900 -25.89300 2.01200   1.000 28.92966 ? 74  GLN A OE1 1 
ATOM   419  N  NE2 . GLN A 1 59  ? -20.85600 -27.64700 0.65400   1.000 30.74384 ? 74  GLN A NE2 1 
ATOM   420  N  N   . GLN A 1 60  ? -22.11600 -26.59300 7.55000   1.000 12.98199 ? 75  GLN A N   1 
ATOM   421  C  CA  . GLN A 1 60  ? -22.95300 -26.60300 8.74500   1.000 12.84290 ? 75  GLN A CA  1 
ATOM   422  C  C   . GLN A 1 60  ? -23.17200 -25.16200 9.19000   1.000 13.65926 ? 75  GLN A C   1 
ATOM   423  O  O   . GLN A 1 60  ? -22.66200 -24.71000 10.21600  1.000 12.22821 ? 75  GLN A O   1 
ATOM   424  C  CB  . GLN A 1 60  ? -22.30600 -27.45200 9.85100   1.000 13.41372 ? 75  GLN A CB  1 
ATOM   425  C  CG  . GLN A 1 60  ? -22.23900 -28.93900 9.51200   1.000 14.08657 ? 75  GLN A CG  1 
ATOM   426  C  CD  . GLN A 1 60  ? -21.80100 -29.79600 10.69300  1.000 21.86261 ? 75  GLN A CD  1 
ATOM   427  O  OE1 . GLN A 1 60  ? -21.81400 -29.34500 11.84000  1.000 26.61005 ? 75  GLN A OE1 1 
ATOM   428  N  NE2 . GLN A 1 60  ? -21.41900 -31.03700 10.41800  1.000 23.16631 ? 75  GLN A NE2 1 
ATOM   429  N  N   . HIS A 1 61  ? -23.95100 -24.43500 8.38500   1.000 15.84489 ? 76  HIS A N   1 
ATOM   430  C  CA  . HIS A 1 61  ? -24.05100 -22.99400 8.56500   1.000 15.45969 ? 76  HIS A CA  1 
ATOM   431  C  C   . HIS A 1 61  ? -24.75000 -22.62400 9.86400   1.000 13.79450 ? 76  HIS A C   1 
ATOM   432  O  O   . HIS A 1 61  ? -24.39900 -21.61200 10.47600  1.000 12.06698 ? 76  HIS A O   1 
ATOM   433  C  CB  . HIS A 1 61  ? -24.77500 -22.37200 7.38100   1.000 17.89048 ? 76  HIS A CB  1 
ATOM   434  C  CG  . HIS A 1 61  ? -24.15100 -22.70600 6.06700   1.000 19.89868 ? 76  HIS A CG  1 
ATOM   435  N  ND1 . HIS A 1 61  ? -24.42300 -23.87600 5.39300   1.000 20.57501 ? 76  HIS A ND1 1 
ATOM   436  C  CD2 . HIS A 1 61  ? -23.25300 -22.03200 5.31000   1.000 24.46855 ? 76  HIS A CD2 1 
ATOM   437  C  CE1 . HIS A 1 61  ? -23.72400 -23.90600 4.27200   1.000 22.62543 ? 76  HIS A CE1 1 
ATOM   438  N  NE2 . HIS A 1 61  ? -23.00800 -22.79800 4.19600   1.000 22.56276 ? 76  HIS A NE2 1 
ATOM   439  N  N   . GLU A 1 62  ? -25.73000 -23.42100 10.29900  1.000 13.85530 ? 77  GLU A N   1 
ATOM   440  C  CA  . GLU A 1 62  ? -26.38900 -23.14200 11.57200  1.000 13.77014 ? 77  GLU A CA  1 
ATOM   441  C  C   . GLU A 1 62  ? -25.40700 -23.22500 12.73900  1.000 15.26484 ? 77  GLU A C   1 
ATOM   442  O  O   . GLU A 1 62  ? -25.42000 -22.37100 13.63600  1.000 14.32971 ? 77  GLU A O   1 
ATOM   443  C  CB  . GLU A 1 62  ? -27.55900 -24.10600 11.78000  1.000 19.44104 ? 77  GLU A CB  1 
ATOM   444  N  N   . GLN A 1 63  ? -24.54600 -24.24800 12.74900  1.000 13.82727 ? 78  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 63  ? -23.53100 -24.34500 13.79500  1.000 12.43991 ? 78  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 63  ? -22.50100 -23.23300 13.66800  1.000 12.95178 ? 78  GLN A C   1 
ATOM   447  O  O   . GLN A 1 63  ? -22.00100 -22.72900 14.67700  1.000 11.21510 ? 78  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 63  ? -22.84400 -25.71300 13.74600  1.000 15.40932 ? 78  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 63  ? -23.71200 -26.87900 14.23000  1.000 18.03161 ? 78  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 63  ? -24.88200 -27.19000 13.30900  1.000 24.07064 ? 78  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 63  ? -24.75300 -27.18200 12.08200  1.000 27.96646 ? 78  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 63  ? -26.03700 -27.46400 13.90300  1.000 31.62220 ? 78  GLN A NE2 1 
ATOM   453  N  N   . ALA A 1 64  ? -22.15300 -22.85800 12.43100  1.000 10.93902 ? 79  ALA A N   1 
ATOM   454  C  CA  . ALA A 1 64  ? -21.22300 -21.74900 12.22200  1.000 11.86617 ? 79  ALA A CA  1 
ATOM   455  C  C   . ALA A 1 64  ? -21.80300 -20.43300 12.73400  1.000 11.46107 ? 79  ALA A C   1 
ATOM   456  O  O   . ALA A 1 64  ? -21.09700 -19.64000 13.36800  1.000 10.01860 ? 79  ALA A O   1 
ATOM   457  C  CB  . ALA A 1 64  ? -20.87500 -21.63800 10.73300  1.000 11.32994 ? 79  ALA A CB  1 
ATOM   458  N  N   . LEU A 1 65  ? -23.08900 -20.18900 12.47700  1.000 10.93768 ? 80  LEU A N   1 
ATOM   459  C  CA  . LEU A 1 65  ? -23.69800 -18.93800 12.91200  1.000 11.10969 ? 80  LEU A CA  1 
ATOM   460  C  C   . LEU A 1 65  ? -23.68700 -18.83100 14.42900  1.000 11.29652 ? 80  LEU A C   1 
ATOM   461  O  O   . LEU A 1 65  ? -23.37600 -17.76900 14.98000  1.000 10.83637 ? 80  LEU A O   1 
ATOM   462  C  CB  . LEU A 1 65  ? -25.12000 -18.83100 12.37300  1.000 15.06059 ? 80  LEU A CB  1 
ATOM   463  C  CG  . LEU A 1 65  ? -25.84600 -17.52100 12.67700  1.000 18.29524 ? 80  LEU A CG  1 
ATOM   464  C  CD1 . LEU A 1 65  ? -26.54500 -17.01800 11.42400  1.000 21.76470 ? 80  LEU A CD1 1 
ATOM   465  C  CD2 . LEU A 1 65  ? -26.84600 -17.73400 13.78900  1.000 22.91966 ? 80  LEU A CD2 1 
ATOM   466  N  N   . ALA A 1 66  ? -24.00000 -19.93500 15.11600  1.000 12.12544 ? 81  ALA A N   1 
ATOM   467  C  CA  . ALA A 1 66  ? -23.98200 -19.93600 16.57700  1.000 13.31458 ? 81  ALA A CA  1 
ATOM   468  C  C   . ALA A 1 66  ? -22.60600 -19.57800 17.12200  1.000 11.37178 ? 81  ALA A C   1 
ATOM   469  O  O   . ALA A 1 66  ? -22.50600 -18.84600 18.11500  1.000 10.37521 ? 81  ALA A O   1 
ATOM   470  C  CB  . ALA A 1 66  ? -24.43000 -21.29900 17.10900  1.000 12.74707 ? 81  ALA A CB  1 
ATOM   471  N  N   . ASP A 1 67  ? -21.53400 -20.09200 16.50100  1.000 11.82306 ? 82  ASP A N   1 
ATOM   472  C  CA  . ASP A 1 67  ? -20.18800 -19.76600 16.96700  1.000 10.93306 ? 82  ASP A CA  1 
ATOM   473  C  C   . ASP A 1 67  ? -19.85100 -18.30700 16.69400  1.000 11.49804 ? 82  ASP A C   1 
ATOM   474  O  O   . ASP A 1 67  ? -19.16800 -17.66200 17.49700  1.000 9.48721  ? 82  ASP A O   1 
ATOM   475  C  CB  . ASP A 1 67  ? -19.14900 -20.67500 16.30500  1.000 7.85832  ? 82  ASP A CB  1 
ATOM   476  C  CG  . ASP A 1 67  ? -18.91900 -21.94900 17.07900  1.000 11.58594 ? 82  ASP A CG  1 
ATOM   477  O  OD1 . ASP A 1 67  ? -19.28700 -21.98500 18.27900  1.000 11.00431 ? 82  ASP A OD1 1 
ATOM   478  O  OD2 . ASP A 1 67  ? -18.34600 -22.90300 16.50100  1.000 10.13117 ? 82  ASP A OD2 1 
ATOM   479  N  N   . CYS A 1 68  ? -20.31500 -17.76800 15.56700  1.000 10.69430 ? 83  CYS A N   1 
ATOM   480  C  CA  . CYS A 1 68  ? -20.11400 -16.34500 15.32300  1.000 11.01952 ? 83  CYS A CA  1 
ATOM   481  C  C   . CYS A 1 68  ? -20.77400 -15.51100 16.41400  1.000 9.82891  ? 83  CYS A C   1 
ATOM   482  O  O   . CYS A 1 68  ? -20.20700 -14.50900 16.86600  1.000 10.45871 ? 83  CYS A O   1 
ATOM   483  C  CB  . CYS A 1 68  ? -20.66200 -15.95000 13.95400  1.000 9.24019  ? 83  CYS A CB  1 
ATOM   484  S  SG  . CYS A 1 68  ? -19.72700 -16.60000 12.56100  1.000 10.85858 ? 83  CYS A SG  1 
ATOM   485  N  N   . ARG A 1 69  ? -21.97400 -15.90600 16.84800  1.000 9.91954  ? 84  ARG A N   1 
ATOM   486  C  CA  . ARG A 1 69  ? -22.63700 -15.18600 17.93500  1.000 10.57816 ? 84  ARG A CA  1 
ATOM   487  C  C   . ARG A 1 69  ? -21.85700 -15.30400 19.24300  1.000 12.53258 ? 84  ARG A C   1 
ATOM   488  O  O   . ARG A 1 69  ? -21.70500 -14.31700 19.98000  1.000 11.43645 ? 84  ARG A O   1 
ATOM   489  C  CB  . ARG A 1 69  ? -24.06700 -15.69500 18.12000  1.000 13.97738 ? 84  ARG A CB  1 
ATOM   490  C  CG  . ARG A 1 69  ? -24.99200 -15.43100 16.95000  1.000 13.55424 ? 84  ARG A CG  1 
ATOM   491  C  CD  . ARG A 1 69  ? -25.33200 -13.96100 16.82300  1.000 13.79290 ? 84  ARG A CD  1 
ATOM   492  N  NE  . ARG A 1 69  ? -26.25700 -13.74800 15.72100  1.000 15.37122 ? 84  ARG A NE  1 
ATOM   493  C  CZ  . ARG A 1 69  ? -26.23200 -12.68400 14.93300  1.000 16.18708 ? 84  ARG A CZ  1 
ATOM   494  N  NH1 . ARG A 1 69  ? -25.36500 -11.70300 15.13400  1.000 14.45296 ? 84  ARG A NH1 1 
ATOM   495  N  NH2 . ARG A 1 69  ? -27.08600 -12.61100 13.91200  1.000 17.96860 ? 84  ARG A NH2 1 
ATOM   496  N  N   . ARG A 1 70  ? -21.34200 -16.49800 19.55100  1.000 10.39891 ? 85  ARG A N   1 
ATOM   497  C  CA  . ARG A 1 70  ? -20.51800 -16.63600 20.75000  1.000 11.71040 ? 85  ARG A CA  1 
ATOM   498  C  C   . ARG A 1 70  ? -19.27900 -15.75000 20.67500  1.000 10.47117 ? 85  ARG A C   1 
ATOM   499  O  O   . ARG A 1 70  ? -18.92100 -15.09000 21.66000  1.000 13.69006 ? 85  ARG A O   1 
ATOM   500  C  CB  . ARG A 1 70  ? -20.13700 -18.10500 20.95500  1.000 11.53582 ? 85  ARG A CB  1 
ATOM   501  C  CG  . ARG A 1 70  ? -21.32500 -18.96000 21.34900  1.000 14.77538 ? 85  ARG A CG  1 
ATOM   502  C  CD  . ARG A 1 70  ? -21.07100 -20.44300 21.11800  1.000 18.97223 ? 85  ARG A CD  1 
ATOM   503  N  NE  . ARG A 1 70  ? -22.32400 -21.18900 21.15400  1.000 23.04138 ? 85  ARG A NE  1 
ATOM   504  C  CZ  . ARG A 1 70  ? -22.65200 -22.13600 20.28600  1.000 24.10777 ? 85  ARG A CZ  1 
ATOM   505  N  NH1 . ARG A 1 70  ? -21.83400 -22.48300 19.30000  1.000 10.68299 ? 85  ARG A NH1 1 
ATOM   506  N  NH2 . ARG A 1 70  ? -23.83100 -22.74200 20.40600  1.000 27.38805 ? 85  ARG A NH2 1 
ATOM   507  N  N   . ALA A 1 71  ? -18.62300 -15.70700 19.50800  1.000 11.27554 ? 86  ALA A N   1 
ATOM   508  C  CA  . ALA A 1 71  ? -17.45200 -14.85000 19.33600  1.000 9.42080  ? 86  ALA A CA  1 
ATOM   509  C  C   . ALA A 1 71  ? -17.80700 -13.38200 19.51700  1.000 10.81381 ? 86  ALA A C   1 
ATOM   510  O  O   . ALA A 1 71  ? -17.07400 -12.64200 20.17500  1.000 11.82148 ? 86  ALA A O   1 
ATOM   511  C  CB  . ALA A 1 71  ? -16.83000 -15.05900 17.95200  1.000 9.20032  ? 86  ALA A CB  1 
ATOM   512  N  N   . LEU A 1 72  ? -18.92100 -12.94300 18.92400  1.000 11.50150 ? 87  LEU A N   1 
ATOM   513  C  CA  . LEU A 1 72  ? -19.28900 -11.52900 18.98900  1.000 10.96435 ? 87  LEU A CA  1 
ATOM   514  C  C   . LEU A 1 72  ? -19.62300 -11.08900 20.41100  1.000 12.15922 ? 87  LEU A C   1 
ATOM   515  O  O   . LEU A 1 72  ? -19.42400 -9.92100  20.75500  1.000 13.64738 ? 87  LEU A O   1 
ATOM   516  C  CB  . LEU A 1 72  ? -20.46500 -11.24900 18.05600  1.000 11.47533 ? 87  LEU A CB  1 
ATOM   517  C  CG  . LEU A 1 72  ? -20.11100 -11.30300 16.56700  1.000 11.89640 ? 87  LEU A CG  1 
ATOM   518  C  CD1 . LEU A 1 72  ? -21.35100 -11.35700 15.67000  1.000 12.85598 ? 87  LEU A CD1 1 
ATOM   519  C  CD2 . LEU A 1 72  ? -19.23800 -10.09300 16.20100  1.000 13.70444 ? 87  LEU A CD2 1 
ATOM   520  N  N   A GLU A 1 73  ? -20.16200 -11.99400 21.23400  0.505 13.20016 ? 88  GLU A N   1 
ATOM   521  N  N   B GLU A 1 73  ? -20.13600 -11.99900 21.24300  0.495 13.32764 ? 88  GLU A N   1 
ATOM   522  C  CA  A GLU A 1 73  ? -20.37900 -11.68100 22.64300  0.505 13.32106 ? 88  GLU A CA  1 
ATOM   523  C  CA  B GLU A 1 73  ? -20.38600 -11.65400 22.63600  0.495 13.26339 ? 88  GLU A CA  1 
ATOM   524  C  C   A GLU A 1 73  ? -19.06300 -11.39700 23.35000  0.505 13.57133 ? 88  GLU A C   1 
ATOM   525  C  C   B GLU A 1 73  ? -19.08600 -11.46000 23.40700  0.495 13.74231 ? 88  GLU A C   1 
ATOM   526  O  O   A GLU A 1 73  ? -18.99700 -10.54000 24.24200  0.505 15.31882 ? 88  GLU A O   1 
ATOM   527  O  O   B GLU A 1 73  ? -19.05800 -10.72200 24.40100  0.495 15.45720 ? 88  GLU A O   1 
ATOM   528  C  CB  A GLU A 1 73  ? -21.10800 -12.83400 23.33600  0.505 14.17041 ? 88  GLU A CB  1 
ATOM   529  C  CB  B GLU A 1 73  ? -21.24500 -12.73500 23.29500  0.495 14.20848 ? 88  GLU A CB  1 
ATOM   530  C  CG  A GLU A 1 73  ? -22.57900 -12.92600 22.98700  0.505 14.24501 ? 88  GLU A CG  1 
ATOM   531  C  CG  B GLU A 1 73  ? -21.77400 -12.35900 24.66500  0.495 14.96573 ? 88  GLU A CG  1 
ATOM   532  C  CD  A GLU A 1 73  ? -23.22600 -14.21600 23.44900  0.505 16.69700 ? 88  GLU A CD  1 
ATOM   533  C  CD  B GLU A 1 73  ? -22.78900 -13.35600 25.18000  0.495 16.38515 ? 88  GLU A CD  1 
ATOM   534  O  OE1 A GLU A 1 73  ? -22.50300 -15.17800 23.79400  0.505 18.32697 ? 88  GLU A OE1 1 
ATOM   535  O  OE1 B GLU A 1 73  ? -23.77300 -13.63100 24.45800  0.495 16.82990 ? 88  GLU A OE1 1 
ATOM   536  O  OE2 A GLU A 1 73  ? -24.47300 -14.26600 23.45900  0.505 17.56280 ? 88  GLU A OE2 1 
ATOM   537  O  OE2 B GLU A 1 73  ? -22.60200 -13.86400 26.30600  0.495 20.27251 ? 88  GLU A OE2 1 
ATOM   538  N  N   . LEU A 1 74  ? -18.00700 -12.11500 22.97300  1.000 13.36644 ? 89  LEU A N   1 
ATOM   539  C  CA  . LEU A 1 74  ? -16.70500 -11.94700 23.60600  1.000 13.42981 ? 89  LEU A CA  1 
ATOM   540  C  C   . LEU A 1 74  ? -15.88800 -10.83000 22.98100  1.000 13.99482 ? 89  LEU A C   1 
ATOM   541  O  O   . LEU A 1 74  ? -15.10500 -10.17700 23.67900  1.000 17.77594 ? 89  LEU A O   1 
ATOM   542  C  CB  . LEU A 1 74  ? -15.91400 -13.25700 23.52900  1.000 12.66319 ? 89  LEU A CB  1 
ATOM   543  C  CG  . LEU A 1 74  ? -16.40200 -14.40500 24.40500  1.000 14.13574 ? 89  LEU A CG  1 
ATOM   544  C  CD1 . LEU A 1 74  ? -15.78800 -15.71000 23.93900  1.000 16.13465 ? 89  LEU A CD1 1 
ATOM   545  C  CD2 . LEU A 1 74  ? -16.02000 -14.12800 25.84800  1.000 15.94407 ? 89  LEU A CD2 1 
ATOM   546  N  N   . ASP A 1 75  ? -16.04700 -10.59700 21.67500  1.000 15.17398 ? 90  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 75  ? -15.24100 -9.61800  20.94000  1.000 13.88071 ? 90  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 75  ? -16.15400 -8.97800  19.89900  1.000 12.06629 ? 90  ASP A C   1 
ATOM   549  O  O   . ASP A 1 75  ? -16.23900 -9.45200  18.76100  1.000 11.69013 ? 90  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 75  ? -14.02500 -10.28300 20.30300  1.000 13.83032 ? 90  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 75  ? -13.22000 -9.32900  19.43100  1.000 14.78102 ? 90  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 75  ? -13.43700 -8.10100  19.51100  1.000 15.30113 ? 90  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 75  ? -12.36600 -9.82100  18.66000  1.000 17.14668 ? 90  ASP A OD2 1 
ATOM   554  N  N   . GLY A 1 76  ? -16.83400 -7.90200  20.30100  1.000 14.14774 ? 91  GLY A N   1 
ATOM   555  C  CA  . GLY A 1 76  ? -17.73600 -7.21100  19.39200  1.000 11.84364 ? 91  GLY A CA  1 
ATOM   556  C  C   . GLY A 1 76  ? -17.04800 -6.59300  18.19200  1.000 13.25763 ? 91  GLY A C   1 
ATOM   557  O  O   . GLY A 1 76  ? -17.73500 -6.16900  17.25500  1.000 11.47657 ? 91  GLY A O   1 
ATOM   558  N  N   . GLN A 1 77  ? -15.71700 -6.51900  18.19800  1.000 11.22278 ? 92  GLN A N   1 
ATOM   559  C  CA  . GLN A 1 77  ? -14.96900 -5.90200  17.11000  1.000 12.43028 ? 92  GLN A CA  1 
ATOM   560  C  C   . GLN A 1 77  ? -14.37900 -6.93200  16.16000  1.000 11.67579 ? 92  GLN A C   1 
ATOM   561  O  O   . GLN A 1 77  ? -13.58800 -6.56300  15.28800  1.000 13.26325 ? 92  GLN A O   1 
ATOM   562  C  CB  . GLN A 1 77  ? -13.84700 -5.02200  17.66700  1.000 12.59347 ? 92  GLN A CB  1 
ATOM   563  C  CG  . GLN A 1 77  ? -14.30900 -3.92800  18.62800  1.000 15.39809 ? 92  GLN A CG  1 
ATOM   564  C  CD  . GLN A 1 77  ? -15.30700 -2.97600  18.00200  1.000 16.56466 ? 92  GLN A CD  1 
ATOM   565  O  OE1 . GLN A 1 77  ? -14.99700 -2.26000  17.04300  1.000 18.17284 ? 92  GLN A OE1 1 
ATOM   566  N  NE2 . GLN A 1 77  ? -16.51600 -2.95100  18.55000  1.000 13.90969 ? 92  GLN A NE2 1 
ATOM   567  N  N   . SER A 1 78  ? -14.75900 -8.20300  16.29200  1.000 10.98995 ? 93  SER A N   1 
ATOM   568  C  CA  . SER A 1 78  ? -14.12100 -9.26800  15.52300  1.000 9.95926  ? 93  SER A CA  1 
ATOM   569  C  C   . SER A 1 78  ? -14.49000 -9.16700  14.04800  1.000 11.16100 ? 93  SER A C   1 
ATOM   570  O  O   . SER A 1 78  ? -15.65500 -9.34200  13.67900  1.000 10.13858 ? 93  SER A O   1 
ATOM   571  C  CB  . SER A 1 78  ? -14.52000 -10.63700 16.06500  1.000 10.82460 ? 93  SER A CB  1 
ATOM   572  O  OG  . SER A 1 78  ? -14.05400 -11.66900 15.20500  1.000 10.96387 ? 93  SER A OG  1 
ATOM   573  N  N   . VAL A 1 79  ? -13.48000 -8.92600  13.21300  1.000 9.37324  ? 94  VAL A N   1 
ATOM   574  C  CA  . VAL A 1 79  ? -13.67500 -8.89500  11.76500  1.000 10.07826 ? 94  VAL A CA  1 
ATOM   575  C  C   . VAL A 1 79  ? -14.17400 -10.24600 11.26900  1.000 8.97502  ? 94  VAL A C   1 
ATOM   576  O  O   . VAL A 1 79  ? -15.17400 -10.33000 10.54100  1.000 11.07477 ? 94  VAL A O   1 
ATOM   577  C  CB  . VAL A 1 79  ? -12.36200 -8.48700  11.06900  1.000 10.07899 ? 94  VAL A CB  1 
ATOM   578  C  CG1 . VAL A 1 79  ? -12.45800 -8.67500  9.55700   1.000 11.42579 ? 94  VAL A CG1 1 
ATOM   579  C  CG2 . VAL A 1 79  ? -12.04000 -7.04200  11.38900  1.000 11.16992 ? 94  VAL A CG2 1 
ATOM   580  N  N   . LYS A 1 80  ? -13.48400 -11.32400 11.65100  1.000 10.07035 ? 95  LYS A N   1 
ATOM   581  C  CA  . LYS A 1 80  ? -13.83800 -12.64500 11.14500  1.000 8.78460  ? 95  LYS A CA  1 
ATOM   582  C  C   . LYS A 1 80  ? -15.20800 -13.08600 11.63500  1.000 8.90022  ? 95  LYS A C   1 
ATOM   583  O  O   . LYS A 1 80  ? -15.94100 -13.75000 10.90100  1.000 9.31062  ? 95  LYS A O   1 
ATOM   584  C  CB  . LYS A 1 80  ? -12.76700 -13.66500 11.52200  1.000 11.52542 ? 95  LYS A CB  1 
ATOM   585  C  CG  . LYS A 1 80  ? -11.54400 -13.56500 10.60600  1.000 15.51621 ? 95  LYS A CG  1 
ATOM   586  C  CD  . LYS A 1 80  ? -10.48200 -14.60500 10.88300  1.000 16.09023 ? 95  LYS A CD  1 
ATOM   587  C  CE  . LYS A 1 80  ? -9.28200  -14.34100 10.00100  1.000 19.78346 ? 95  LYS A CE  1 
ATOM   588  N  NZ  . LYS A 1 80  ? -8.27900  -15.41300 10.12100  1.000 17.35322 ? 95  LYS A NZ  1 
ATOM   589  N  N   . ALA A 1 81  ? -15.58700 -12.73200 12.86300  1.000 9.61544  ? 96  ALA A N   1 
ATOM   590  C  CA  . ALA A 1 81  ? -16.93000 -13.09800 13.30300  1.000 8.84113  ? 96  ALA A CA  1 
ATOM   591  C  C   . ALA A 1 81  ? -17.98500 -12.45100 12.40700  1.000 9.61700  ? 96  ALA A C   1 
ATOM   592  O  O   . ALA A 1 81  ? -18.94400 -13.10900 11.98800  1.000 8.44218  ? 96  ALA A O   1 
ATOM   593  C  CB  . ALA A 1 81  ? -17.14500 -12.72000 14.76600  1.000 10.00592 ? 96  ALA A CB  1 
ATOM   594  N  N   . HIS A 1 82  ? -17.80200 -11.17300 12.06800  1.000 8.43931  ? 97  HIS A N   1 
ATOM   595  C  CA  . HIS A 1 82  ? -18.74500 -10.52200 11.16100  1.000 8.08128  ? 97  HIS A CA  1 
ATOM   596  C  C   . HIS A 1 82  ? -18.67400 -11.11600 9.76100   1.000 8.62731  ? 97  HIS A C   1 
ATOM   597  O  O   . HIS A 1 82  ? -19.70300 -11.26700 9.09500   1.000 8.12636  ? 97  HIS A O   1 
ATOM   598  C  CB  . HIS A 1 82  ? -18.48500 -9.02300  11.10600  1.000 9.43545  ? 97  HIS A CB  1 
ATOM   599  C  CG  . HIS A 1 82  ? -18.93900 -8.27800  12.32400  1.000 9.14193  ? 97  HIS A CG  1 
ATOM   600  N  ND1 . HIS A 1 82  ? -18.14000 -8.09700  13.43500  1.000 9.01567  ? 97  HIS A ND1 1 
ATOM   601  C  CD2 . HIS A 1 82  ? -20.11000 -7.65900  12.59600  1.000 10.44328 ? 97  HIS A CD2 1 
ATOM   602  C  CE1 . HIS A 1 82  ? -18.79800 -7.39100  14.33300  1.000 9.98676  ? 97  HIS A CE1 1 
ATOM   603  N  NE2 . HIS A 1 82  ? -19.99600 -7.11200  13.85200  1.000 9.62270  ? 97  HIS A NE2 1 
ATOM   604  N  N   . PHE A 1 83  ? -17.46600 -11.41300 9.27300   1.000 9.32178  ? 98  PHE A N   1 
ATOM   605  C  CA  . PHE A 1 83  ? -17.34500 -11.94300 7.91800   1.000 9.61457  ? 98  PHE A CA  1 
ATOM   606  C  C   . PHE A 1 83  ? -17.99000 -13.32100 7.81200   1.000 10.61071 ? 98  PHE A C   1 
ATOM   607  O  O   . PHE A 1 83  ? -18.78100 -13.58600 6.89400   1.000 11.37051 ? 98  PHE A O   1 
ATOM   608  C  CB  . PHE A 1 83  ? -15.87300 -12.00800 7.52100   1.000 8.38580  ? 98  PHE A CB  1 
ATOM   609  C  CG  . PHE A 1 83  ? -15.64500 -12.51100 6.12000   1.000 9.75644  ? 98  PHE A CG  1 
ATOM   610  C  CD1 . PHE A 1 83  ? -15.66700 -11.63900 5.04800   1.000 10.05164 ? 98  PHE A CD1 1 
ATOM   611  C  CD2 . PHE A 1 83  ? -15.40800 -13.85800 5.88100   1.000 12.43250 ? 98  PHE A CD2 1 
ATOM   612  C  CE1 . PHE A 1 83  ? -15.47200 -12.09800 3.76500   1.000 11.15207 ? 98  PHE A CE1 1 
ATOM   613  C  CE2 . PHE A 1 83  ? -15.21000 -14.32600 4.60900   1.000 11.88496 ? 98  PHE A CE2 1 
ATOM   614  C  CZ  . PHE A 1 83  ? -15.23200 -13.44900 3.54300   1.000 10.55451 ? 98  PHE A CZ  1 
ATOM   615  N  N   . PHE A 1 84  ? -17.64500 -14.22700 8.73000   1.000 9.23240  ? 99  PHE A N   1 
ATOM   616  C  CA  . PHE A 1 84  ? -18.21800 -15.56400 8.66400   1.000 10.48739 ? 99  PHE A CA  1 
ATOM   617  C  C   . PHE A 1 84  ? -19.72400 -15.53300 8.89100   1.000 9.74208  ? 99  PHE A C   1 
ATOM   618  O  O   . PHE A 1 84  ? -20.45400 -16.32900 8.29200   1.000 9.84467  ? 99  PHE A O   1 
ATOM   619  C  CB  . PHE A 1 84  ? -17.53500 -16.48400 9.68000   1.000 9.92401  ? 99  PHE A CB  1 
ATOM   620  C  CG  . PHE A 1 84  ? -16.06700 -16.69300 9.41600   1.000 10.75263 ? 99  PHE A CG  1 
ATOM   621  C  CD1 . PHE A 1 84  ? -15.55700 -16.63100 8.11900   1.000 13.00559 ? 99  PHE A CD1 1 
ATOM   622  C  CD2 . PHE A 1 84  ? -15.19300 -16.92900 10.46700  1.000 10.98389 ? 99  PHE A CD2 1 
ATOM   623  C  CE1 . PHE A 1 84  ? -14.19600 -16.82400 7.88200   1.000 13.25862 ? 99  PHE A CE1 1 
ATOM   624  C  CE2 . PHE A 1 84  ? -13.83900 -17.12200 10.24200  1.000 11.71643 ? 99  PHE A CE2 1 
ATOM   625  C  CZ  . PHE A 1 84  ? -13.33900 -17.06900 8.95200   1.000 12.69337 ? 99  PHE A CZ  1 
ATOM   626  N  N   . LEU A 1 85  ? -20.20900 -14.62000 9.74000   1.000 7.46292  ? 100 LEU A N   1 
ATOM   627  C  CA  . LEU A 1 85  ? -21.65000 -14.46300 9.91700   1.000 11.30339 ? 100 LEU A CA  1 
ATOM   628  C  C   . LEU A 1 85  ? -22.32100 -14.05600 8.60900   1.000 10.16582 ? 100 LEU A C   1 
ATOM   629  O  O   . LEU A 1 85  ? -23.37500 -14.59400 8.25300   1.000 11.57099 ? 100 LEU A O   1 
ATOM   630  C  CB  . LEU A 1 85  ? -21.93100 -13.43000 11.01100  1.000 10.28261 ? 100 LEU A CB  1 
ATOM   631  C  CG  . LEU A 1 85  ? -23.38900 -13.06800 11.26900  1.000 12.55264 ? 100 LEU A CG  1 
ATOM   632  C  CD1 . LEU A 1 85  ? -24.15800 -14.32500 11.64400  1.000 14.70449 ? 100 LEU A CD1 1 
ATOM   633  C  CD2 . LEU A 1 85  ? -23.44500 -12.04700 12.38900  1.000 14.32787 ? 100 LEU A CD2 1 
ATOM   634  N  N   . GLY A 1 86  ? -21.73000 -13.10100 7.88600   1.000 11.47649 ? 101 GLY A N   1 
ATOM   635  C  CA  . GLY A 1 86  ? -22.26500 -12.73600 6.58500   1.000 11.62133 ? 101 GLY A CA  1 
ATOM   636  C  C   . GLY A 1 86  ? -22.29500 -13.90300 5.61600   1.000 12.00134 ? 101 GLY A C   1 
ATOM   637  O  O   . GLY A 1 86  ? -23.23900 -14.04500 4.83100   1.000 13.42988 ? 101 GLY A O   1 
ATOM   638  N  N   . GLN A 1 87  ? -21.26600 -14.76100 5.65800   1.000 12.52708 ? 102 GLN A N   1 
ATOM   639  C  CA  . GLN A 1 87  ? -21.26800 -15.93400 4.78800   1.000 12.79529 ? 102 GLN A CA  1 
ATOM   640  C  C   . GLN A 1 87  ? -22.40500 -16.87500 5.15500   1.000 14.17527 ? 102 GLN A C   1 
ATOM   641  O  O   . GLN A 1 87  ? -23.07800 -17.42100 4.27300   1.000 15.83520 ? 102 GLN A O   1 
ATOM   642  C  CB  . GLN A 1 87  ? -19.92600 -16.66600 4.85800   1.000 12.41938 ? 102 GLN A CB  1 
ATOM   643  C  CG  . GLN A 1 87  ? -18.75700 -15.86700 4.35000   1.000 13.60986 ? 102 GLN A CG  1 
ATOM   644  C  CD  . GLN A 1 87  ? -18.92300 -15.45800 2.90800   1.000 22.37531 ? 102 GLN A CD  1 
ATOM   645  O  OE1 . GLN A 1 87  ? -18.70200 -14.30100 2.55300   1.000 25.62012 ? 102 GLN A OE1 1 
ATOM   646  N  NE2 . GLN A 1 87  ? -19.32100 -16.40500 2.06500   1.000 23.13434 ? 102 GLN A NE2 1 
ATOM   647  N  N   . CYS A 1 88  ? -22.63900 -17.06700 6.45600   1.000 16.56701 ? 103 CYS A N   1 
ATOM   648  C  CA  . CYS A 1 88  ? -23.77700 -17.86900 6.89500   1.000 16.59976 ? 103 CYS A CA  1 
ATOM   649  C  C   . CYS A 1 88  ? -25.08300 -17.30100 6.36300   1.000 19.46598 ? 103 CYS A C   1 
ATOM   650  O  O   . CYS A 1 88  ? -25.93900 -18.03600 5.84800   1.000 20.92062 ? 103 CYS A O   1 
ATOM   651  C  CB  . CYS A 1 88  ? -23.82600 -17.92300 8.41900   1.000 19.10819 ? 103 CYS A CB  1 
ATOM   652  S  SG  . CYS A 1 88  ? -22.53300 -18.89900 9.16400   1.000 23.82457 ? 103 CYS A SG  1 
ATOM   653  N  N   . GLN A 1 89  ? -25.26100 -15.98600 6.50200   1.000 15.04025 ? 104 GLN A N   1 
ATOM   654  C  CA  . GLN A 1 89  ? -26.51700 -15.36500 6.10300   1.000 15.30402 ? 104 GLN A CA  1 
ATOM   655  C  C   . GLN A 1 89  ? -26.71600 -15.43500 4.60000   1.000 16.16867 ? 104 GLN A C   1 
ATOM   656  O  O   . GLN A 1 89  ? -27.85100 -15.57700 4.13100   1.000 18.48239 ? 104 GLN A O   1 
ATOM   657  C  CB  . GLN A 1 89  ? -26.55300 -13.92600 6.61000   1.000 13.38690 ? 104 GLN A CB  1 
ATOM   658  C  CG  . GLN A 1 89  ? -26.70200 -13.89100 8.12400   1.000 13.73695 ? 104 GLN A CG  1 
ATOM   659  C  CD  . GLN A 1 89  ? -26.36300 -12.54500 8.72100   1.000 16.67212 ? 104 GLN A CD  1 
ATOM   660  O  OE1 . GLN A 1 89  ? -25.61200 -11.76500 8.13000   1.000 15.30517 ? 104 GLN A OE1 1 
ATOM   661  N  NE2 . GLN A 1 89  ? -26.91300 -12.26700 9.91000   1.000 17.92814 ? 104 GLN A NE2 1 
ATOM   662  N  N   . LEU A 1 90  ? -25.62500 -15.37200 3.83900   1.000 16.08451 ? 105 LEU A N   1 
ATOM   663  C  CA  . LEU A 1 90  ? -25.71400 -15.56000 2.39700   1.000 17.27687 ? 105 LEU A CA  1 
ATOM   664  C  C   . LEU A 1 90  ? -26.30400 -16.92400 2.06300   1.000 19.26657 ? 105 LEU A C   1 
ATOM   665  O  O   . LEU A 1 90  ? -27.19500 -17.03700 1.21000   1.000 20.01662 ? 105 LEU A O   1 
ATOM   666  C  CB  . LEU A 1 90  ? -24.32100 -15.39100 1.78500   1.000 16.27791 ? 105 LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 90  ? -24.20300 -15.21400 0.27600   1.000 23.97649 ? 105 LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 90  ? -25.07900 -14.06300 -0.19700  1.000 22.82629 ? 105 LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 90  ? -22.75000 -14.98100 -0.09500  1.000 23.12187 ? 105 LEU A CD2 1 
ATOM   670  N  N   . GLU A 1 91  ? -25.83900 -17.97300 2.74500   1.000 19.02139 ? 106 GLU A N   1 
ATOM   671  C  CA  . GLU A 1 91  ? -26.37700 -19.30700 2.49400   1.000 18.58169 ? 106 GLU A CA  1 
ATOM   672  C  C   . GLU A 1 91  ? -27.84800 -19.39600 2.88200   1.000 24.31014 ? 106 GLU A C   1 
ATOM   673  O  O   . GLU A 1 91  ? -28.62600 -20.09400 2.21800   1.000 23.91534 ? 106 GLU A O   1 
ATOM   674  C  CB  . GLU A 1 91  ? -25.55800 -20.35400 3.24900   1.000 24.76632 ? 106 GLU A CB  1 
ATOM   675  C  CG  . GLU A 1 91  ? -25.87400 -21.79400 2.85900   1.000 26.93906 ? 106 GLU A CG  1 
ATOM   676  C  CD  . GLU A 1 91  ? -27.06400 -22.38500 3.60500   1.000 35.35456 ? 106 GLU A CD  1 
ATOM   677  O  OE1 . GLU A 1 91  ? -27.42700 -21.85400 4.67800   1.000 30.29254 ? 106 GLU A OE1 1 
ATOM   678  O  OE2 . GLU A 1 91  ? -27.63700 -23.38500 3.11500   1.000 40.58333 ? 106 GLU A OE2 1 
ATOM   679  N  N   . MET A 1 92  ? -28.24500 -18.68800 3.93700   1.000 21.75487 ? 107 MET A N   1 
ATOM   680  C  CA  . MET A 1 92  ? -29.62600 -18.63700 4.39300   1.000 20.35094 ? 107 MET A CA  1 
ATOM   681  C  C   . MET A 1 92  ? -30.49800 -17.71500 3.55100   1.000 18.95920 ? 107 MET A C   1 
ATOM   682  O  O   . MET A 1 92  ? -31.69900 -17.60500 3.82300   1.000 21.95510 ? 107 MET A O   1 
ATOM   683  C  CB  . MET A 1 92  ? -29.65100 -18.19600 5.86200   1.000 23.22225 ? 107 MET A CB  1 
ATOM   684  C  CG  . MET A 1 92  ? -28.77400 -19.06400 6.75400   1.000 26.35287 ? 107 MET A CG  1 
ATOM   685  S  SD  . MET A 1 92  ? -28.35400 -18.34200 8.36600   1.000 50.80245 ? 107 MET A SD  1 
ATOM   686  C  CE  . MET A 1 92  ? -29.40900 -16.88800 8.40900   1.000 31.98358 ? 107 MET A CE  1 
ATOM   687  N  N   . GLU A 1 93  ? -29.92000 -17.04900 2.54700   1.000 22.11106 ? 108 GLU A N   1 
ATOM   688  C  CA  . GLU A 1 93  ? -30.64300 -16.14800 1.65200   1.000 20.02554 ? 108 GLU A CA  1 
ATOM   689  C  C   . GLU A 1 93  ? -31.17900 -14.92400 2.38800   1.000 21.05692 ? 108 GLU A C   1 
ATOM   690  O  O   . GLU A 1 93  ? -32.16900 -14.31800 1.97200   1.000 23.46436 ? 108 GLU A O   1 
ATOM   691  C  CB  . GLU A 1 93  ? -31.76000 -16.88800 0.90600   1.000 24.74116 ? 108 GLU A CB  1 
ATOM   692  C  CG  . GLU A 1 93  ? -31.21900 -18.03900 0.06400   1.000 26.79918 ? 108 GLU A CG  1 
ATOM   693  C  CD  . GLU A 1 93  ? -32.30000 -18.89900 -0.56300  1.000 40.68825 ? 108 GLU A CD  1 
ATOM   694  O  OE1 . GLU A 1 93  ? -33.43100 -18.40300 -0.76800  1.000 40.98858 ? 108 GLU A OE1 1 
ATOM   695  O  OE2 . GLU A 1 93  ? -32.01000 -20.08100 -0.85800  1.000 41.93720 ? 108 GLU A OE2 1 
ATOM   696  N  N   . SER A 1 94  ? -30.52300 -14.55900 3.49400   1.000 19.36668 ? 109 SER A N   1 
ATOM   697  C  CA  . SER A 1 94  ? -30.75800 -13.28400 4.17500   1.000 19.94568 ? 109 SER A CA  1 
ATOM   698  C  C   . SER A 1 94  ? -29.76400 -12.28000 3.60300   1.000 17.91164 ? 109 SER A C   1 
ATOM   699  O  O   . SER A 1 94  ? -28.74400 -11.95500 4.20700   1.000 16.23295 ? 109 SER A O   1 
ATOM   700  C  CB  . SER A 1 94  ? -30.59300 -13.43300 5.68200   1.000 22.33230 ? 109 SER A CB  1 
ATOM   701  O  OG  . SER A 1 94  ? -31.56700 -14.29900 6.22600   1.000 31.45310 ? 109 SER A OG  1 
ATOM   702  N  N   . TYR A 1 95  ? -30.07000 -11.78800 2.40000   1.000 17.71147 ? 110 TYR A N   1 
ATOM   703  C  CA  . TYR A 1 95  ? -29.05300 -11.06200 1.64500   1.000 16.96720 ? 110 TYR A CA  1 
ATOM   704  C  C   . TYR A 1 95  ? -28.74200 -9.70400  2.25300   1.000 15.72033 ? 110 TYR A C   1 
ATOM   705  O  O   . TYR A 1 95  ? -27.57500 -9.30500  2.30700   1.000 15.42077 ? 110 TYR A O   1 
ATOM   706  C  CB  . TYR A 1 95  ? -29.48500 -10.89900 0.18900   1.000 16.23586 ? 110 TYR A CB  1 
ATOM   707  C  CG  . TYR A 1 95  ? -29.68100 -12.21800 -0.51200  1.000 18.07651 ? 110 TYR A CG  1 
ATOM   708  C  CD1 . TYR A 1 95  ? -28.60700 -13.06800 -0.74500  1.000 19.45764 ? 110 TYR A CD1 1 
ATOM   709  C  CD2 . TYR A 1 95  ? -30.94100 -12.62000 -0.94000  1.000 22.07981 ? 110 TYR A CD2 1 
ATOM   710  C  CE1 . TYR A 1 95  ? -28.78600 -14.28300 -1.38200  1.000 21.39304 ? 110 TYR A CE1 1 
ATOM   711  C  CE2 . TYR A 1 95  ? -31.12800 -13.83000 -1.57200  1.000 18.76381 ? 110 TYR A CE2 1 
ATOM   712  C  CZ  . TYR A 1 95  ? -30.04600 -14.65300 -1.79700  1.000 20.22221 ? 110 TYR A CZ  1 
ATOM   713  O  OH  . TYR A 1 95  ? -30.23200 -15.85900 -2.43300  1.000 29.48357 ? 110 TYR A OH  1 
ATOM   714  N  N   . ASP A 1 96  ? -29.76500 -8.95700  2.67800   1.000 16.24102 ? 111 ASP A N   1 
ATOM   715  C  CA  . ASP A 1 96  ? -29.50100 -7.63600  3.23800   1.000 17.76860 ? 111 ASP A CA  1 
ATOM   716  C  C   . ASP A 1 96  ? -28.68400 -7.73600  4.52000   1.000 16.30771 ? 111 ASP A C   1 
ATOM   717  O  O   . ASP A 1 96  ? -27.78300 -6.91900  4.75400   1.000 13.99157 ? 111 ASP A O   1 
ATOM   718  C  CB  . ASP A 1 96  ? -30.81000 -6.89500  3.49500   1.000 20.27670 ? 111 ASP A CB  1 
ATOM   719  C  CG  . ASP A 1 96  ? -31.56100 -6.58000  2.22300   1.000 26.56736 ? 111 ASP A CG  1 
ATOM   720  O  OD1 . ASP A 1 96  ? -30.93700 -6.57000  1.13900   1.000 26.49444 ? 111 ASP A OD1 1 
ATOM   721  O  OD2 . ASP A 1 96  ? -32.78200 -6.33200  2.30900   1.000 36.49558 ? 111 ASP A OD2 1 
ATOM   722  N  N   . GLU A 1 97  ? -28.99100 -8.72400  5.36900   1.000 16.97915 ? 112 GLU A N   1 
ATOM   723  C  CA  . GLU A 1 97  ? -28.19300 -8.93500  6.58000   1.000 14.02793 ? 112 GLU A CA  1 
ATOM   724  C  C   . GLU A 1 97  ? -26.76400 -9.32900  6.23100   1.000 14.03567 ? 112 GLU A C   1 
ATOM   725  O  O   . GLU A 1 97  ? -25.81100 -8.86100  6.86500   1.000 12.80890 ? 112 GLU A O   1 
ATOM   726  C  CB  . GLU A 1 97  ? -28.80500 -10.02400 7.45600   1.000 18.40474 ? 112 GLU A CB  1 
ATOM   727  C  CG  . GLU A 1 97  ? -30.14000 -9.71200  8.08000   1.000 24.05529 ? 112 GLU A CG  1 
ATOM   728  C  CD  . GLU A 1 97  ? -30.53900 -10.78800 9.06800   1.000 34.84959 ? 112 GLU A CD  1 
ATOM   729  O  OE1 . GLU A 1 97  ? -30.90800 -11.89200 8.61400   1.000 39.39817 ? 112 GLU A OE1 1 
ATOM   730  O  OE2 . GLU A 1 97  ? -30.45000 -10.54800 10.29400  1.000 34.41497 ? 112 GLU A OE2 1 
ATOM   731  N  N   . ALA A 1 98  ? -26.60400 -10.21200 5.23700   1.000 12.38312 ? 113 ALA A N   1 
ATOM   732  C  CA  . ALA A 1 98  ? -25.27200 -10.67600 4.86800   1.000 11.90049 ? 113 ALA A CA  1 
ATOM   733  C  C   . ALA A 1 98  ? -24.42000 -9.52100  4.37000   1.000 10.26663 ? 113 ALA A C   1 
ATOM   734  O  O   . ALA A 1 98  ? -23.25600 -9.38200  4.76500   1.000 11.68000 ? 113 ALA A O   1 
ATOM   735  C  CB  . ALA A 1 98  ? -25.36800 -11.77800 3.80800   1.000 13.74213 ? 113 ALA A CB  1 
ATOM   736  N  N   . ILE A 1 99  ? -24.99600 -8.66500  3.52500   1.000 8.86001  ? 114 ILE A N   1 
ATOM   737  C  CA  . ILE A 1 99  ? -24.27900 -7.49400  3.02300   1.000 10.82638 ? 114 ILE A CA  1 
ATOM   738  C  C   . ILE A 1 99  ? -23.90700 -6.55200  4.16500   1.000 12.79862 ? 114 ILE A C   1 
ATOM   739  O  O   . ILE A 1 99  ? -22.78800 -6.02100  4.21200   1.000 11.69543 ? 114 ILE A O   1 
ATOM   740  C  CB  . ILE A 1 99  ? -25.12000 -6.79200  1.94500   1.000 12.49646 ? 114 ILE A CB  1 
ATOM   741  C  CG1 . ILE A 1 99  ? -25.23100 -7.70500  0.72200   1.000 13.41799 ? 114 ILE A CG1 1 
ATOM   742  C  CG2 . ILE A 1 99  ? -24.53600 -5.41100  1.61200   1.000 14.73723 ? 114 ILE A CG2 1 
ATOM   743  C  CD1 . ILE A 1 99  ? -26.27300 -7.27800  -0.28100  1.000 16.67456 ? 114 ILE A CD1 1 
ATOM   744  N  N   . ALA A 1 100 ? -24.82700 -6.33900  5.11000   1.000 9.77489  ? 115 ALA A N   1 
ATOM   745  C  CA  . ALA A 1 100 ? -24.52800 -5.47400  6.24900   1.000 12.66022 ? 115 ALA A CA  1 
ATOM   746  C  C   . ALA A 1 100 ? -23.34600 -6.00200  7.05500   1.000 11.06493 ? 115 ALA A C   1 
ATOM   747  O  O   . ALA A 1 100 ? -22.45800 -5.23400  7.44800   1.000 11.15342 ? 115 ALA A O   1 
ATOM   748  C  CB  . ALA A 1 100 ? -25.77000 -5.33300  7.13200   1.000 13.52947 ? 115 ALA A CB  1 
ATOM   749  N  N   . ASN A 1 101 ? -23.31100 -7.31300  7.31100   1.000 9.49995  ? 116 ASN A N   1 
ATOM   750  C  CA  . ASN A 1 101 ? -22.21600 -7.86600  8.10000   1.000 9.11956  ? 116 ASN A CA  1 
ATOM   751  C  C   . ASN A 1 101 ? -20.90800 -7.85000  7.32200   1.000 9.13005  ? 116 ASN A C   1 
ATOM   752  O  O   . ASN A 1 101 ? -19.83700 -7.63900  7.90600   1.000 9.07426  ? 116 ASN A O   1 
ATOM   753  C  CB  . ASN A 1 101 ? -22.56400 -9.28200  8.56100   1.000 10.24154 ? 116 ASN A CB  1 
ATOM   754  C  CG  . ASN A 1 101 ? -23.36800 -9.27400  9.85000   1.000 12.47209 ? 116 ASN A CG  1 
ATOM   755  O  OD1 . ASN A 1 101 ? -22.88700 -8.81300  10.87900  1.000 12.35203 ? 116 ASN A OD1 1 
ATOM   756  N  ND2 . ASN A 1 101 ? -24.59400 -9.77800  9.79800   1.000 12.68243 ? 116 ASN A ND2 1 
ATOM   757  N  N   . LEU A 1 102 ? -20.96900 -8.08000  6.01100   1.000 8.55146  ? 117 LEU A N   1 
ATOM   758  C  CA  . LEU A 1 102 ? -19.75700 -7.99300  5.20000   1.000 9.30407  ? 117 LEU A CA  1 
ATOM   759  C  C   . LEU A 1 102 ? -19.22800 -6.55900  5.13900   1.000 10.40524 ? 117 LEU A C   1 
ATOM   760  O  O   . LEU A 1 102 ? -18.01000 -6.34000  5.20900   1.000 10.35680 ? 117 LEU A O   1 
ATOM   761  C  CB  . LEU A 1 102 ? -20.02700 -8.54800  3.79800   1.000 10.50664 ? 117 LEU A CB  1 
ATOM   762  C  CG  . LEU A 1 102 ? -20.27400 -10.05900 3.77800   1.000 9.87622  ? 117 LEU A CG  1 
ATOM   763  C  CD1 . LEU A 1 102 ? -20.79200 -10.47600 2.39400   1.000 11.26614 ? 117 LEU A CD1 1 
ATOM   764  C  CD2 . LEU A 1 102 ? -19.01800 -10.84600 4.14600   1.000 9.88808  ? 117 LEU A CD2 1 
ATOM   765  N  N   . GLN A 1 103 ? -20.12000 -5.56400  5.02100   1.000 10.11295 ? 118 GLN A N   1 
ATOM   766  C  CA  . GLN A 1 103 ? -19.67800 -4.17300  5.06300   1.000 11.21882 ? 118 GLN A CA  1 
ATOM   767  C  C   . GLN A 1 103 ? -19.12100 -3.82500  6.43900   1.000 10.12854 ? 118 GLN A C   1 
ATOM   768  O  O   . GLN A 1 103 ? -18.14900 -3.06900  6.55100   1.000 12.22147 ? 118 GLN A O   1 
ATOM   769  C  CB  . GLN A 1 103 ? -20.83200 -3.23100  4.70100   1.000 13.66580 ? 118 GLN A CB  1 
ATOM   770  C  CG  . GLN A 1 103 ? -21.27700 -3.28600  3.24100   1.000 14.68091 ? 118 GLN A CG  1 
ATOM   771  C  CD  . GLN A 1 103 ? -22.56800 -2.52900  2.99800   1.000 25.88168 ? 118 GLN A CD  1 
ATOM   772  O  OE1 . GLN A 1 103 ? -23.43800 -2.47100  3.86900   1.000 24.26178 ? 118 GLN A OE1 1 
ATOM   773  N  NE2 . GLN A 1 103 ? -22.70600 -1.94900  1.80700   1.000 23.18458 ? 118 GLN A NE2 1 
ATOM   774  N  N   . ARG A 1 104 ? -19.70700 -4.39200  7.49900   1.000 9.11658  ? 119 ARG A N   1 
ATOM   775  C  CA  . ARG A 1 104 ? -19.18000 -4.13900  8.83700   1.000 11.23750 ? 119 ARG A CA  1 
ATOM   776  C  C   . ARG A 1 104 ? -17.80500 -4.77400  9.00600   1.000 11.66939 ? 119 ARG A C   1 
ATOM   777  O  O   . ARG A 1 104 ? -16.90500 -4.17000  9.59700   1.000 10.70082 ? 119 ARG A O   1 
ATOM   778  C  CB  . ARG A 1 104 ? -20.15400 -4.66300  9.89800   1.000 11.11915 ? 119 ARG A CB  1 
ATOM   779  C  CG  . ARG A 1 104 ? -19.69400 -4.44400  11.34300  1.000 9.70879  ? 119 ARG A CG  1 
ATOM   780  C  CD  . ARG A 1 104 ? -19.55300 -2.96600  11.67800  1.000 12.11575 ? 119 ARG A CD  1 
ATOM   781  N  NE  . ARG A 1 104 ? -19.32300 -2.76500  13.10800  1.000 10.51751 ? 119 ARG A NE  1 
ATOM   782  C  CZ  . ARG A 1 104 ? -18.77300 -1.68000  13.63500  1.000 12.20752 ? 119 ARG A CZ  1 
ATOM   783  N  NH1 . ARG A 1 104 ? -18.42700 -0.64200  12.88900  1.000 15.26816 ? 119 ARG A NH1 1 
ATOM   784  N  NH2 . ARG A 1 104 ? -18.54900 -1.63800  14.94800  1.000 11.46652 ? 119 ARG A NH2 1 
ATOM   785  N  N   . ALA A 1 105 ? -17.62400 -5.99200  8.49100   1.000 8.98498  ? 120 ALA A N   1 
ATOM   786  C  CA  . ALA A 1 105 ? -16.29400 -6.59700  8.49900   1.000 10.17251 ? 120 ALA A CA  1 
ATOM   787  C  C   . ALA A 1 105 ? -15.29600 -5.72700  7.74300   1.000 9.30374  ? 120 ALA A C   1 
ATOM   788  O  O   . ALA A 1 105 ? -14.16100 -5.53700  8.19400   1.000 11.36984 ? 120 ALA A O   1 
ATOM   789  C  CB  . ALA A 1 105 ? -16.34000 -7.99900  7.88800   1.000 9.49707  ? 120 ALA A CB  1 
ATOM   790  N  N   . TYR A 1 106 ? -15.70500 -5.18500  6.59500   1.000 9.03497  ? 121 TYR A N   1 
ATOM   791  C  CA  . TYR A 1 106 ? -14.81500 -4.31900  5.83000   1.000 11.16129 ? 121 TYR A CA  1 
ATOM   792  C  C   . TYR A 1 106 ? -14.41400 -3.09700  6.64600   1.000 11.85777 ? 121 TYR A C   1 
ATOM   793  O  O   . TYR A 1 106 ? -13.23600 -2.72900  6.69900   1.000 13.07844 ? 121 TYR A O   1 
ATOM   794  C  CB  . TYR A 1 106 ? -15.49700 -3.88800  4.53600   1.000 11.20158 ? 121 TYR A CB  1 
ATOM   795  C  CG  . TYR A 1 106 ? -14.64900 -3.00500  3.66600   1.000 17.91719 ? 121 TYR A CG  1 
ATOM   796  C  CD1 . TYR A 1 106 ? -13.75600 -3.55100  2.75900   1.000 19.34606 ? 121 TYR A CD1 1 
ATOM   797  C  CD2 . TYR A 1 106 ? -14.74000 -1.61800  3.75100   1.000 21.55317 ? 121 TYR A CD2 1 
ATOM   798  C  CE1 . TYR A 1 106 ? -12.98300 -2.74800  1.95500   1.000 24.92743 ? 121 TYR A CE1 1 
ATOM   799  C  CE2 . TYR A 1 106 ? -13.96700 -0.80800  2.95800   1.000 23.47405 ? 121 TYR A CE2 1 
ATOM   800  C  CZ  . TYR A 1 106 ? -13.09200 -1.37800  2.05800   1.000 27.36086 ? 121 TYR A CZ  1 
ATOM   801  O  OH  . TYR A 1 106 ? -12.31900 -0.56500  1.25800   1.000 33.62514 ? 121 TYR A OH  1 
ATOM   802  N  N   . SER A 1 107 ? -15.39400 -2.46300  7.29700   1.000 11.69743 ? 122 SER A N   1 
ATOM   803  C  CA  . SER A 1 107 ? -15.13000 -1.26900  8.08700   1.000 10.87391 ? 122 SER A CA  1 
ATOM   804  C  C   . SER A 1 107 ? -14.22300 -1.56700  9.26400   1.000 13.23568 ? 122 SER A C   1 
ATOM   805  O  O   . SER A 1 107 ? -13.32300 -0.77600  9.57700   1.000 16.20245 ? 122 SER A O   1 
ATOM   806  C  CB  . SER A 1 107 ? -16.44400 -0.67100  8.58100   1.000 16.34881 ? 122 SER A CB  1 
ATOM   807  O  OG  . SER A 1 107 ? -17.10200 -0.01600  7.51500   1.000 24.80272 ? 122 SER A OG  1 
ATOM   808  N  N   . LEU A 1 108 ? -14.46300 -2.69300  9.94300   1.000 10.93887 ? 123 LEU A N   1 
ATOM   809  C  CA  . LEU A 1 108 ? -13.64000 -3.05200  11.09300  1.000 12.34200 ? 123 LEU A CA  1 
ATOM   810  C  C   . LEU A 1 108 ? -12.22400 -3.40000  10.66300  1.000 13.14391 ? 123 LEU A C   1 
ATOM   811  O  O   . LEU A 1 108 ? -11.25600 -3.06100  11.35600  1.000 15.13009 ? 123 LEU A O   1 
ATOM   812  C  CB  . LEU A 1 108 ? -14.27400 -4.22400  11.84400  1.000 11.36231 ? 123 LEU A CB  1 
ATOM   813  C  CG  . LEU A 1 108 ? -15.59800 -3.97400  12.56000  1.000 12.76394 ? 123 LEU A CG  1 
ATOM   814  C  CD1 . LEU A 1 108 ? -16.21700 -5.30600  12.93200  1.000 13.34585 ? 123 LEU A CD1 1 
ATOM   815  C  CD2 . LEU A 1 108 ? -15.38100 -3.14300  13.81200  1.000 16.59939 ? 123 LEU A CD2 1 
ATOM   816  N  N   . ALA A 1 109 ? -12.08400 -4.07800  9.51900   1.000 13.13031 ? 124 ALA A N   1 
ATOM   817  C  CA  . ALA A 1 109 ? -10.75600 -4.41600  9.02300   1.000 13.09384 ? 124 ALA A CA  1 
ATOM   818  C  C   . ALA A 1 109 ? -9.97100  -3.16000  8.67100   1.000 16.47408 ? 124 ALA A C   1 
ATOM   819  O  O   . ALA A 1 109 ? -8.77100  -3.07200  8.95000   1.000 16.86302 ? 124 ALA A O   1 
ATOM   820  C  CB  . ALA A 1 109 ? -10.87400 -5.34300  7.81200   1.000 14.88040 ? 124 ALA A CB  1 
ATOM   821  N  N   . LYS A 1 110 ? -10.63700 -2.17000  8.07300   1.000 14.81368 ? 125 LYS A N   1 
ATOM   822  C  CA  . LYS A 1 110 ? -9.98100  -0.89600  7.78700   1.000 16.27929 ? 125 LYS A CA  1 
ATOM   823  C  C   . LYS A 1 110 ? -9.56500  -0.19100  9.07300   1.000 17.99345 ? 125 LYS A C   1 
ATOM   824  O  O   . LYS A 1 110 ? -8.43500  0.30200   9.18600   1.000 16.42603 ? 125 LYS A O   1 
ATOM   825  C  CB  . LYS A 1 110 ? -10.92100 -0.01900  6.95600   1.000 16.48697 ? 125 LYS A CB  1 
ATOM   826  C  CG  . LYS A 1 110 ? -10.38600 1.36500   6.60900   1.000 21.69673 ? 125 LYS A CG  1 
ATOM   827  C  CD  . LYS A 1 110 ? -11.38800 2.11900   5.73600   1.000 25.38794 ? 125 LYS A CD  1 
ATOM   828  C  CE  . LYS A 1 110 ? -10.83800 3.45100   5.25000   1.000 28.52305 ? 125 LYS A CE  1 
ATOM   829  N  NZ  . LYS A 1 110 ? -11.90500 4.27300   4.60200   1.000 25.62604 ? 125 LYS A NZ  1 
ATOM   830  N  N   . GLU A 1 111 ? -10.46300 -0.15300  10.06100  1.000 16.81897 ? 126 GLU A N   1 
ATOM   831  C  CA  . GLU A 1 111 ? -10.16800 0.47400   11.34600  1.000 20.92923 ? 126 GLU A CA  1 
ATOM   832  C  C   . GLU A 1 111 ? -9.00200  -0.21500  12.04900  1.000 20.89376 ? 126 GLU A C   1 
ATOM   833  O  O   . GLU A 1 111 ? -8.17200  0.45100   12.68200  1.000 23.65081 ? 126 GLU A O   1 
ATOM   834  C  CB  . GLU A 1 111 ? -11.44000 0.44400   12.20600  1.000 19.98255 ? 126 GLU A CB  1 
ATOM   835  C  CG  . GLU A 1 111 ? -11.33100 0.98700   13.61600  1.000 30.87973 ? 126 GLU A CG  1 
ATOM   836  C  CD  . GLU A 1 111 ? -12.59700 0.70900   14.41500  1.000 35.81121 ? 126 GLU A CD  1 
ATOM   837  O  OE1 . GLU A 1 111 ? -13.65500 0.46200   13.79400  1.000 37.32654 ? 126 GLU A OE1 1 
ATOM   838  O  OE2 . GLU A 1 111 ? -12.53800 0.71900   15.66200  1.000 41.24514 ? 126 GLU A OE2 1 
ATOM   839  N  N   . GLN A 1 112 ? -8.90400  -1.53800  11.92100  1.000 17.94679 ? 127 GLN A N   1 
ATOM   840  C  CA  . GLN A 1 112 ? -7.86500  -2.31200  12.58100  1.000 17.44220 ? 127 GLN A CA  1 
ATOM   841  C  C   . GLN A 1 112 ? -6.61500  -2.48800  11.72600  1.000 19.75712 ? 127 GLN A C   1 
ATOM   842  O  O   . GLN A 1 112 ? -5.67200  -3.15500  12.16600  1.000 22.99848 ? 127 GLN A O   1 
ATOM   843  C  CB  . GLN A 1 112 ? -8.41800  -3.68300  12.99100  1.000 17.35755 ? 127 GLN A CB  1 
ATOM   844  C  CG  . GLN A 1 112 ? -9.46400  -3.61200  14.09800  1.000 16.58920 ? 127 GLN A CG  1 
ATOM   845  C  CD  . GLN A 1 112 ? -10.29000 -4.88300  14.21700  1.000 14.65083 ? 127 GLN A CD  1 
ATOM   846  O  OE1 . GLN A 1 112 ? -9.78200  -5.99400  14.03300  1.000 16.62754 ? 127 GLN A OE1 1 
ATOM   847  N  NE2 . GLN A 1 112 ? -11.57400 -4.72400  14.51100  1.000 13.90748 ? 127 GLN A NE2 1 
ATOM   848  N  N   . ARG A 1 113 ? -6.58400  -1.90400  10.52700  1.000 19.45398 ? 128 ARG A N   1 
ATOM   849  C  CA  . ARG A 1 113 ? -5.43300  -2.00100  9.62500   1.000 20.30466 ? 128 ARG A CA  1 
ATOM   850  C  C   . ARG A 1 113 ? -5.09500  -3.45900  9.31900   1.000 22.22982 ? 128 ARG A C   1 
ATOM   851  O  O   . ARG A 1 113 ? -3.92700  -3.85300  9.28300   1.000 25.55174 ? 128 ARG A O   1 
ATOM   852  C  CB  . ARG A 1 113 ? -4.22100  -1.25900  10.19400  1.000 26.46746 ? 128 ARG A CB  1 
ATOM   853  N  N   . LEU A 1 114 ? -6.13100  -4.26200  9.10100   1.000 17.46219 ? 129 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 114 ? -5.97700  -5.66700  8.75000   1.000 21.22655 ? 129 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 114 ? -5.96100  -5.82200  7.24000   1.000 22.19145 ? 129 LEU A C   1 
ATOM   856  O  O   . LEU A 1 114 ? -6.70900  -5.14800  6.52600   1.000 26.50630 ? 129 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 114 ? -7.11400  -6.50400  9.33700   1.000 24.14573 ? 129 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 114 ? -7.20400  -6.55700  10.86000  1.000 18.93124 ? 129 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 114 ? -8.30300  -7.51200  11.28600  1.000 17.33785 ? 129 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 114 ? -5.87500  -6.98800  11.42300  1.000 25.11207 ? 129 LEU A CD2 1 
ATOM   861  N  N   . ASN A 1 115 ? -5.12400  -6.73000  6.76100   1.000 21.56784 ? 130 ASN A N   1 
ATOM   862  C  CA  . ASN A 1 115 ? -4.95200  -6.96400  5.33200   1.000 23.89596 ? 130 ASN A CA  1 
ATOM   863  C  C   . ASN A 1 115 ? -5.43500  -8.36900  4.99600   1.000 22.40070 ? 130 ASN A C   1 
ATOM   864  O  O   . ASN A 1 115 ? -4.79300  -9.35800  5.37200   1.000 25.63060 ? 130 ASN A O   1 
ATOM   865  C  CB  . ASN A 1 115 ? -3.49300  -6.78000  4.92600   1.000 27.73606 ? 130 ASN A CB  1 
ATOM   866  C  CG  . ASN A 1 115 ? -3.28300  -6.92900  3.43200   1.000 31.95790 ? 130 ASN A CG  1 
ATOM   867  O  OD1 . ASN A 1 115 ? -4.22500  -6.80200  2.64600   1.000 29.88130 ? 130 ASN A OD1 1 
ATOM   868  N  ND2 . ASN A 1 115 ? -2.04400  -7.19800  3.03100   1.000 34.11679 ? 130 ASN A ND2 1 
ATOM   869  N  N   . PHE A 1 116 ? -6.55500  -8.45800  4.27800   1.000 21.37117 ? 131 PHE A N   1 
ATOM   870  C  CA  . PHE A 1 116 ? -7.02900  -9.72700  3.74100   1.000 20.93432 ? 131 PHE A CA  1 
ATOM   871  C  C   . PHE A 1 116 ? -7.08700  -9.68800  2.22100   1.000 20.99607 ? 131 PHE A C   1 
ATOM   872  O  O   . PHE A 1 116 ? -7.92500  -10.35000 1.60900   1.000 18.73589 ? 131 PHE A O   1 
ATOM   873  C  CB  . PHE A 1 116 ? -8.39100  -10.09600 4.31900   1.000 20.55076 ? 131 PHE A CB  1 
ATOM   874  C  CG  . PHE A 1 116 ? -8.39100  -10.23300 5.80800   1.000 20.35254 ? 131 PHE A CG  1 
ATOM   875  C  CD1 . PHE A 1 116 ? -7.67700  -11.25200 6.42600   1.000 20.86112 ? 131 PHE A CD1 1 
ATOM   876  C  CD2 . PHE A 1 116 ? -9.09900  -9.34100  6.59900   1.000 22.43056 ? 131 PHE A CD2 1 
ATOM   877  C  CE1 . PHE A 1 116 ? -7.67600  -11.38000 7.80300   1.000 21.81756 ? 131 PHE A CE1 1 
ATOM   878  C  CE2 . PHE A 1 116 ? -9.10200  -9.46400  7.97900   1.000 20.47447 ? 131 PHE A CE2 1 
ATOM   879  C  CZ  . PHE A 1 116 ? -8.39300  -10.48500 8.58400   1.000 18.08311 ? 131 PHE A CZ  1 
ATOM   880  N  N   . GLY A 1 117 ? -6.19300  -8.92500  1.60300   1.000 20.64299 ? 132 GLY A N   1 
ATOM   881  C  CA  . GLY A 1 117 ? -6.25600  -8.77400  0.16400   1.000 16.65324 ? 132 GLY A CA  1 
ATOM   882  C  C   . GLY A 1 117 ? -7.60600  -8.21600  -0.22900  1.000 18.66269 ? 132 GLY A C   1 
ATOM   883  O  O   . GLY A 1 117 ? -8.16000  -7.33900  0.43700   1.000 17.77512 ? 132 GLY A O   1 
ATOM   884  N  N   . ASP A 1 118 ? -8.16400  -8.75000  -1.31500  1.000 15.81857 ? 133 ASP A N   1 
ATOM   885  C  CA  . ASP A 1 118 ? -9.46700  -8.31400  -1.79100  1.000 15.77630 ? 133 ASP A CA  1 
ATOM   886  C  C   . ASP A 1 118 ? -10.59800 -9.22000  -1.30700  1.000 13.47686 ? 133 ASP A C   1 
ATOM   887  O  O   . ASP A 1 118 ? -11.69200 -9.19600  -1.88300  1.000 13.13897 ? 133 ASP A O   1 
ATOM   888  C  CB  . ASP A 1 118 ? -9.45500  -8.22800  -3.31600  1.000 14.23478 ? 133 ASP A CB  1 
ATOM   889  C  CG  . ASP A 1 118 ? -10.55200 -7.33700  -3.86100  1.000 19.72511 ? 133 ASP A CG  1 
ATOM   890  O  OD1 . ASP A 1 118 ? -10.74400 -6.22300  -3.31800  1.000 21.25617 ? 133 ASP A OD1 1 
ATOM   891  O  OD2 . ASP A 1 118 ? -11.20600 -7.74500  -4.84800  1.000 19.56420 ? 133 ASP A OD2 1 
ATOM   892  N  N   . ASP A 1 119 ? -10.37300 -9.98300  -0.23100  1.000 14.13479 ? 134 ASP A N   1 
ATOM   893  C  CA  . ASP A 1 119 ? -11.34800 -10.99800 0.17200   1.000 14.14704 ? 134 ASP A CA  1 
ATOM   894  C  C   . ASP A 1 119 ? -12.69100 -10.38100 0.54600   1.000 11.84372 ? 134 ASP A C   1 
ATOM   895  O  O   . ASP A 1 119 ? -13.74700 -10.89000 0.14800   1.000 10.56973 ? 134 ASP A O   1 
ATOM   896  C  CB  . ASP A 1 119 ? -10.80500 -11.82200 1.34000   1.000 13.39743 ? 134 ASP A CB  1 
ATOM   897  C  CG  . ASP A 1 119 ? -9.76400  -12.84100 0.90500   1.000 15.92536 ? 134 ASP A CG  1 
ATOM   898  O  OD1 . ASP A 1 119 ? -9.42900  -12.89600 -0.30300  1.000 16.22482 ? 134 ASP A OD1 1 
ATOM   899  O  OD2 . ASP A 1 119 ? -9.27900  -13.60700 1.77100   1.000 17.72406 ? 134 ASP A OD2 1 
ATOM   900  N  N   . ILE A 1 120 ? -12.68600 -9.29900  1.31700   1.000 11.80261 ? 135 ILE A N   1 
ATOM   901  C  CA  . ILE A 1 120 ? -13.96500 -8.77900  1.80000   1.000 10.91949 ? 135 ILE A CA  1 
ATOM   902  C  C   . ILE A 1 120 ? -14.71200 -8.09500  0.65600   1.000 11.05404 ? 135 ILE A C   1 
ATOM   903  O  O   . ILE A 1 120 ? -15.90500 -8.37900  0.47600   1.000 10.16325 ? 135 ILE A O   1 
ATOM   904  C  CB  . ILE A 1 120 ? -13.78700 -7.85200  3.01300   1.000 10.22258 ? 135 ILE A CB  1 
ATOM   905  C  CG1 . ILE A 1 120 ? -13.07600 -8.59900  4.14300   1.000 11.84880 ? 135 ILE A CG1 1 
ATOM   906  C  CG2 . ILE A 1 120 ? -15.14800 -7.39200  3.50000   1.000 10.26082 ? 135 ILE A CG2 1 
ATOM   907  C  CD1 . ILE A 1 120 ? -12.82000 -7.73100  5.38400   1.000 13.26938 ? 135 ILE A CD1 1 
ATOM   908  N  N   . PRO A 1 121 ? -14.09100 -7.21500  -0.14500  1.000 11.06076 ? 136 PRO A N   1 
ATOM   909  C  CA  . PRO A 1 121 ? -14.81800 -6.69500  -1.31800  1.000 10.75670 ? 136 PRO A CA  1 
ATOM   910  C  C   . PRO A 1 121 ? -15.30500 -7.78600  -2.25900  1.000 12.03135 ? 136 PRO A C   1 
ATOM   911  O  O   . PRO A 1 121 ? -16.41200 -7.67000  -2.80700  1.000 11.70747 ? 136 PRO A O   1 
ATOM   912  C  CB  . PRO A 1 121 ? -13.78400 -5.78500  -1.99700  1.000 13.08505 ? 136 PRO A CB  1 
ATOM   913  C  CG  . PRO A 1 121 ? -12.92000 -5.32800  -0.88600  1.000 13.80777 ? 136 PRO A CG  1 
ATOM   914  C  CD  . PRO A 1 121 ? -12.81900 -6.49200  0.06400   1.000 12.97616 ? 136 PRO A CD  1 
ATOM   915  N  N   . SER A 1 122 ? -14.50800 -8.84800  -2.45600  1.000 12.03514 ? 137 SER A N   1 
ATOM   916  C  CA  . SER A 1 122 ? -14.94100 -9.95500  -3.31400  1.000 12.29095 ? 137 SER A CA  1 
ATOM   917  C  C   . SER A 1 122 ? -16.18700 -10.63400 -2.76000  1.000 11.05193 ? 137 SER A C   1 
ATOM   918  O  O   . SER A 1 122 ? -17.10400 -10.99600 -3.51600  1.000 10.26249 ? 137 SER A O   1 
ATOM   919  C  CB  . SER A 1 122 ? -13.81500 -10.98400 -3.47000  1.000 13.24781 ? 137 SER A CB  1 
ATOM   920  O  OG  . SER A 1 122 ? -12.75700 -10.51200 -4.29100  1.000 15.11400 ? 137 SER A OG  1 
ATOM   921  N  N   . ALA A 1 123 ? -16.23900 -10.81700 -1.43600  1.000 10.93649 ? 138 ALA A N   1 
ATOM   922  C  CA  . ALA A 1 123 ? -17.41500 -11.40800 -0.81400  1.000 12.00074 ? 138 ALA A CA  1 
ATOM   923  C  C   . ALA A 1 123 ? -18.62200 -10.48900 -0.93200  1.000 10.42703 ? 138 ALA A C   1 
ATOM   924  O  O   . ALA A 1 123 ? -19.75100 -10.95800 -1.11000  1.000 11.09927 ? 138 ALA A O   1 
ATOM   925  C  CB  . ALA A 1 123 ? -17.12000 -11.71700 0.65000   1.000 11.23495 ? 138 ALA A CB  1 
ATOM   926  N  N   . LEU A 1 124 ? -18.40500 -9.17400  -0.81300  1.000 11.75848 ? 139 LEU A N   1 
ATOM   927  C  CA  . LEU A 1 124 ? -19.49800 -8.22400  -1.00100  1.000 11.21639 ? 139 LEU A CA  1 
ATOM   928  C  C   . LEU A 1 124 ? -20.05500 -8.30600  -2.41400  1.000 11.63735 ? 139 LEU A C   1 
ATOM   929  O  O   . LEU A 1 124 ? -21.27200 -8.26100  -2.62000  1.000 11.62388 ? 139 LEU A O   1 
ATOM   930  C  CB  . LEU A 1 124 ? -19.01400 -6.80500  -0.70600  1.000 11.39826 ? 139 LEU A CB  1 
ATOM   931  C  CG  . LEU A 1 124 ? -19.06600 -6.43900  0.77700   1.000 13.98224 ? 139 LEU A CG  1 
ATOM   932  C  CD1 . LEU A 1 124 ? -18.18400 -5.22700  1.08500   1.000 12.81955 ? 139 LEU A CD1 1 
ATOM   933  C  CD2 . LEU A 1 124 ? -20.51100 -6.14900  1.14700   1.000 14.13235 ? 139 LEU A CD2 1 
ATOM   934  N  N   . ARG A 1 125 ? -19.17100 -8.40200  -3.40100  1.000 11.46021 ? 140 ARG A N   1 
ATOM   935  C  CA  . ARG A 1 125 ? -19.62400 -8.51600  -4.78200  1.000 12.01079 ? 140 ARG A CA  1 
ATOM   936  C  C   . ARG A 1 125 ? -20.41400 -9.80500  -4.98700  1.000 11.87159 ? 140 ARG A C   1 
ATOM   937  O  O   . ARG A 1 125 ? -21.47100 -9.79500  -5.62000  1.000 11.63404 ? 140 ARG A O   1 
ATOM   938  C  CB  . ARG A 1 125 ? -18.41400 -8.43700  -5.71800  1.000 13.54470 ? 140 ARG A CB  1 
ATOM   939  C  CG  . ARG A 1 125 ? -18.66800 -8.88800  -7.13200  1.000 22.41535 ? 140 ARG A CG  1 
ATOM   940  C  CD  . ARG A 1 125 ? -19.31100 -7.80100  -7.94300  1.000 26.08143 ? 140 ARG A CD  1 
ATOM   941  N  NE  . ARG A 1 125 ? -18.89700 -7.86800  -9.33900  1.000 32.65837 ? 140 ARG A NE  1 
ATOM   942  C  CZ  . ARG A 1 125 ? -18.80900 -6.81400  -10.13600 1.000 31.29562 ? 140 ARG A CZ  1 
ATOM   943  N  NH1 . ARG A 1 125 ? -19.08700 -5.59500  -9.70100  1.000 32.75081 ? 140 ARG A NH1 1 
ATOM   944  N  NH2 . ARG A 1 125 ? -18.43100 -6.98500  -11.40100 1.000 36.13330 ? 140 ARG A NH2 1 
ATOM   945  N  N   . ILE A 1 126 ? -19.93600 -10.92000 -4.42500  1.000 11.02988 ? 141 ILE A N   1 
ATOM   946  C  CA  . ILE A 1 126 ? -20.70100 -12.16500 -4.48300  1.000 11.18045 ? 141 ILE A CA  1 
ATOM   947  C  C   . ILE A 1 126 ? -22.08100 -11.98400 -3.85500  1.000 11.73996 ? 141 ILE A C   1 
ATOM   948  O  O   . ILE A 1 126 ? -23.10100 -12.41600 -4.41100  1.000 12.11257 ? 141 ILE A O   1 
ATOM   949  C  CB  . ILE A 1 126 ? -19.91400 -13.29800 -3.80000  1.000 11.24222 ? 141 ILE A CB  1 
ATOM   950  C  CG1 . ILE A 1 126 ? -18.74100 -13.73900 -4.67400  1.000 11.40301 ? 141 ILE A CG1 1 
ATOM   951  C  CG2 . ILE A 1 126 ? -20.84100 -14.46700 -3.48600  1.000 12.50830 ? 141 ILE A CG2 1 
ATOM   952  C  CD1 . ILE A 1 126 ? -17.75400 -14.63000 -3.96000  1.000 13.90694 ? 141 ILE A CD1 1 
ATOM   953  N  N   . ALA A 1 127 ? -22.13800 -11.35300 -2.67600  1.000 11.18694 ? 142 ALA A N   1 
ATOM   954  C  CA  . ALA A 1 127 ? -23.41200 -11.22800 -1.97900  1.000 10.70355 ? 142 ALA A CA  1 
ATOM   955  C  C   . ALA A 1 127 ? -24.40400 -10.37600 -2.76700  1.000 11.47865 ? 142 ALA A C   1 
ATOM   956  O  O   . ALA A 1 127 ? -25.59500 -10.70000 -2.83000  1.000 11.41901 ? 142 ALA A O   1 
ATOM   957  C  CB  . ALA A 1 127 ? -23.20000 -10.64100 -0.58300  1.000 13.40207 ? 142 ALA A CB  1 
ATOM   958  N  N   . LYS A 1 128 ? -23.93600 -9.28100  -3.36800  1.000 12.50432 ? 143 LYS A N   1 
ATOM   959  C  CA  . LYS A 1 128 ? -24.84300 -8.42300  -4.12200  1.000 12.82881 ? 143 LYS A CA  1 
ATOM   960  C  C   . LYS A 1 128 ? -25.29700 -9.09200  -5.41200  1.000 13.47496 ? 143 LYS A C   1 
ATOM   961  O  O   . LYS A 1 128 ? -26.43900 -8.89200  -5.84200  1.000 14.53755 ? 143 LYS A O   1 
ATOM   962  C  CB  . LYS A 1 128 ? -24.17900 -7.07400  -4.41100  1.000 12.60558 ? 143 LYS A CB  1 
ATOM   963  C  CG  . LYS A 1 128 ? -23.84600 -6.28000  -3.14400  1.000 14.92489 ? 143 LYS A CG  1 
ATOM   964  C  CD  . LYS A 1 128 ? -23.08300 -5.00200  -3.45100  1.000 17.13937 ? 143 LYS A CD  1 
ATOM   965  C  CE  . LYS A 1 128 ? -22.71800 -4.25000  -2.17300  1.000 27.43705 ? 143 LYS A CE  1 
ATOM   966  N  NZ  . LYS A 1 128 ? -21.81600 -3.08300  -2.43400  1.000 36.93228 ? 143 LYS A NZ  1 
ATOM   967  N  N   . LYS A 1 129 ? -24.43000 -9.88300  -6.02000  1.000 12.60882 ? 144 LYS A N   1 
ATOM   968  C  CA  . LYS A 1 129 ? -24.83900 -10.63700 -7.22800  1.000 12.32088 ? 144 LYS A CA  1 
ATOM   969  C  C   . LYS A 1 129 ? -25.91000 -11.67100 -6.86500  1.000 13.27869 ? 144 LYS A C   1 
ATOM   970  O  O   . LYS A 1 129 ? -26.81100 -11.87900 -7.66100  1.000 15.27106 ? 144 LYS A O   1 
ATOM   971  C  CB  . LYS A 1 129 ? -23.64200 -11.35100 -7.85300  1.000 13.46106 ? 144 LYS A CB  1 
ATOM   972  C  CG  . LYS A 1 129 ? -22.70400 -10.48100 -8.67700  1.000 21.29863 ? 144 LYS A CG  1 
ATOM   973  C  CD  . LYS A 1 129 ? -21.35900 -11.13800 -8.90800  1.000 24.09483 ? 144 LYS A CD  1 
ATOM   974  C  CE  . LYS A 1 129 ? -20.54400 -10.48900 -10.00500 1.000 29.75743 ? 144 LYS A CE  1 
ATOM   975  N  NZ  . LYS A 1 129 ? -19.54500 -11.42100 -10.58900 1.000 33.19183 ? 144 LYS A NZ  1 
ATOM   976  N  N   . LYS A 1 130 ? -25.72200 -12.35600 -5.74500  1.000 14.62237 ? 145 LYS A N   1 
ATOM   977  C  CA  . LYS A 1 130 ? -26.71500 -13.35000 -5.34800  1.000 16.34987 ? 145 LYS A CA  1 
ATOM   978  C  C   . LYS A 1 130 ? -28.04500 -12.69400 -5.00700  1.000 15.81146 ? 145 LYS A C   1 
ATOM   979  O  O   . LYS A 1 130 ? -29.10600 -13.22800 -5.34300  1.000 17.88215 ? 145 LYS A O   1 
ATOM   980  C  CB  . LYS A 1 130 ? -26.21400 -14.17400 -4.16200  1.000 16.25944 ? 145 LYS A CB  1 
ATOM   981  C  CG  . LYS A 1 130 ? -25.03000 -15.05800 -4.48400  1.000 19.43208 ? 145 LYS A CG  1 
ATOM   982  C  CD  . LYS A 1 130 ? -25.31900 -15.93700 -5.69100  1.000 24.50128 ? 145 LYS A CD  1 
ATOM   983  C  CE  . LYS A 1 130 ? -26.44200 -16.92700 -5.41200  1.000 26.70603 ? 145 LYS A CE  1 
ATOM   984  N  NZ  . LYS A 1 130 ? -26.92700 -17.55100 -6.67400  1.000 31.07363 ? 145 LYS A NZ  1 
ATOM   985  N  N   . ARG A 1 131 ? -28.01200 -11.53900 -4.33600  1.000 14.35326 ? 146 ARG A N   1 
ATOM   986  C  CA  . ARG A 1 131 ? -29.24900 -10.80600 -4.08400  1.000 15.41189 ? 146 ARG A CA  1 
ATOM   987  C  C   . ARG A 1 131 ? -29.93400 -10.44600 -5.39700  1.000 16.66407 ? 146 ARG A C   1 
ATOM   988  O  O   . ARG A 1 131 ? -31.14200 -10.65600 -5.56600  1.000 16.21896 ? 146 ARG A O   1 
ATOM   989  C  CB  . ARG A 1 131 ? -28.95900 -9.55000  -3.26200  1.000 15.63543 ? 146 ARG A CB  1 
ATOM   990  C  CG  . ARG A 1 131 ? -30.20100 -8.72700  -2.93000  1.000 19.09307 ? 146 ARG A CG  1 
ATOM   991  C  CD  . ARG A 1 131 ? -29.88500 -7.51300  -2.06800  1.000 23.51138 ? 146 ARG A CD  1 
ATOM   992  N  NE  . ARG A 1 131 ? -29.02000 -6.55600  -2.74600  1.000 29.83691 ? 146 ARG A NE  1 
ATOM   993  C  CZ  . ARG A 1 131 ? -28.53600 -5.45100  -2.19000  1.000 31.83919 ? 146 ARG A CZ  1 
ATOM   994  N  NH1 . ARG A 1 131 ? -28.82100 -5.12400  -0.93800  1.000 32.17567 ? 146 ARG A NH1 1 
ATOM   995  N  NH2 . ARG A 1 131 ? -27.74300 -4.65600  -2.90800  1.000 34.15807 ? 146 ARG A NH2 1 
ATOM   996  N  N   . TRP A 1 132 ? -29.17000 -9.90300  -6.34500  1.000 14.54974 ? 147 TRP A N   1 
ATOM   997  C  CA  . TRP A 1 132 ? -29.74000 -9.56700  -7.64600  1.000 15.68696 ? 147 TRP A CA  1 
ATOM   998  C  C   . TRP A 1 132 ? -30.25600 -10.80800 -8.36900  1.000 15.10198 ? 147 TRP A C   1 
ATOM   999  O  O   . TRP A 1 132 ? -31.33700 -10.77600 -8.97100  1.000 17.63960 ? 147 TRP A O   1 
ATOM   1000 C  CB  . TRP A 1 132 ? -28.69600 -8.83000  -8.48500  1.000 14.82228 ? 147 TRP A CB  1 
ATOM   1001 C  CG  . TRP A 1 132 ? -29.14300 -8.55900  -9.89200  1.000 17.08975 ? 147 TRP A CG  1 
ATOM   1002 C  CD1 . TRP A 1 132 ? -28.59400 -9.06600  -11.04100 1.000 18.50798 ? 147 TRP A CD1 1 
ATOM   1003 C  CD2 . TRP A 1 132 ? -30.23800 -7.73200  -10.30200 1.000 17.93888 ? 147 TRP A CD2 1 
ATOM   1004 N  NE1 . TRP A 1 132 ? -29.28200 -8.60200  -12.13800 1.000 19.92817 ? 147 TRP A NE1 1 
ATOM   1005 C  CE2 . TRP A 1 132 ? -30.29100 -7.77800  -11.71300 1.000 17.23008 ? 147 TRP A CE2 1 
ATOM   1006 C  CE3 . TRP A 1 132 ? -31.17500 -6.95000  -9.61600  1.000 19.40391 ? 147 TRP A CE3 1 
ATOM   1007 C  CZ2 . TRP A 1 132 ? -31.24600 -7.08000  -12.44700 1.000 22.02135 ? 147 TRP A CZ2 1 
ATOM   1008 C  CZ3 . TRP A 1 132 ? -32.12200 -6.25500  -10.35100 1.000 22.11556 ? 147 TRP A CZ3 1 
ATOM   1009 C  CH2 . TRP A 1 132 ? -32.14900 -6.32500  -11.74900 1.000 24.56720 ? 147 TRP A CH2 1 
ATOM   1010 N  N   . ASN A 1 133 ? -29.51000 -11.91300 -8.31400  1.000 13.61735 ? 148 ASN A N   1 
ATOM   1011 C  CA  . ASN A 1 133 ? -29.98100 -13.15200 -8.93400  1.000 15.68741 ? 148 ASN A CA  1 
ATOM   1012 C  C   . ASN A 1 133 ? -31.29900 -13.61500 -8.32000  1.000 20.20334 ? 148 ASN A C   1 
ATOM   1013 O  O   . ASN A 1 133 ? -32.16500 -14.14700 -9.02400  1.000 18.95356 ? 148 ASN A O   1 
ATOM   1014 C  CB  . ASN A 1 133 ? -28.92300 -14.25000 -8.80600  1.000 17.31802 ? 148 ASN A CB  1 
ATOM   1015 C  CG  . ASN A 1 133 ? -29.32600 -15.52900 -9.51700  1.000 25.32074 ? 148 ASN A CG  1 
ATOM   1016 O  OD1 . ASN A 1 133 ? -29.29000 -15.60200 -10.74700 1.000 28.86792 ? 148 ASN A OD1 1 
ATOM   1017 N  ND2 . ASN A 1 133 ? -29.71300 -16.54600 -8.74700  1.000 28.99043 ? 148 ASN A ND2 1 
ATOM   1018 N  N   . SER A 1 134 ? -31.47400 -13.41600 -7.00900  1.000 18.61047 ? 149 SER A N   1 
ATOM   1019 C  CA  . SER A 1 134 ? -32.71400 -13.84500 -6.37000  1.000 18.35329 ? 149 SER A CA  1 
ATOM   1020 C  C   . SER A 1 134 ? -33.90200 -13.02500 -6.85800  1.000 20.10839 ? 149 SER A C   1 
ATOM   1021 O  O   . SER A 1 134 ? -35.02100 -13.54800 -6.94600  1.000 20.53176 ? 149 SER A O   1 
ATOM   1022 C  CB  . SER A 1 134 ? -32.57900 -13.76500 -4.84500  1.000 18.90056 ? 149 SER A CB  1 
ATOM   1023 O  OG  . SER A 1 134 ? -32.60800 -12.42500 -4.38300  1.000 24.84779 ? 149 SER A OG  1 
ATOM   1024 N  N   . ILE A 1 135 ? -33.67600 -11.75400 -7.19700  1.000 15.81775 ? 150 ILE A N   1 
ATOM   1025 C  CA  . ILE A 1 135 ? -34.72600 -10.93200 -7.79000  1.000 16.72936 ? 150 ILE A CA  1 
ATOM   1026 C  C   . ILE A 1 135 ? -35.06100 -11.42600 -9.19200  1.000 18.67414 ? 150 ILE A C   1 
ATOM   1027 O  O   . ILE A 1 135 ? -36.23600 -11.53900 -9.56800  1.000 19.12406 ? 150 ILE A O   1 
ATOM   1028 C  CB  . ILE A 1 135 ? -34.28300 -9.45500  -7.78800  1.000 20.58711 ? 150 ILE A CB  1 
ATOM   1029 C  CG1 . ILE A 1 135 ? -34.25600 -8.91000  -6.35600  1.000 19.95900 ? 150 ILE A CG1 1 
ATOM   1030 C  CG2 . ILE A 1 135 ? -35.16200 -8.61300  -8.68500  1.000 20.49954 ? 150 ILE A CG2 1 
ATOM   1031 C  CD1 . ILE A 1 135 ? -33.59500 -7.54600  -6.22900  1.000 22.01803 ? 150 ILE A CD1 1 
ATOM   1032 N  N   . GLU A 1 136 ? -34.03300 -11.74700 -9.98000  1.000 18.66064 ? 151 GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 136 ? -34.25700 -12.17700 -11.35500 1.000 19.20044 ? 151 GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 136 ? -34.97700 -13.52300 -11.41500 1.000 19.32225 ? 151 GLU A C   1 
ATOM   1035 O  O   . GLU A 1 136 ? -35.75900 -13.76900 -12.34100 1.000 22.04155 ? 151 GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 136 ? -32.91700 -12.23700 -12.10000 1.000 18.79533 ? 151 GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 136 ? -32.27000 -10.87200 -12.37500 1.000 21.32675 ? 151 GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 136 ? -32.97500 -10.08600 -13.47900 1.000 32.37094 ? 151 GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 136 ? -34.08900 -9.56300  -13.24100 1.000 32.27423 ? 151 GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 136 ? -32.41300 -9.99500  -14.59400 1.000 37.74128 ? 151 GLU A OE2 1 
ATOM   1041 N  N   . GLU A 1 137 ? -34.74300 -14.39500 -10.43000 1.000 18.01902 ? 152 GLU A N   1 
ATOM   1042 C  CA  . GLU A 1 137 ? -35.38600 -15.70400 -10.38000 1.000 18.34815 ? 152 GLU A CA  1 
ATOM   1043 C  C   . GLU A 1 137 ? -36.87500 -15.64200 -10.06100 1.000 20.03686 ? 152 GLU A C   1 
ATOM   1044 O  O   . GLU A 1 137 ? -37.53800 -16.68700 -10.09900 1.000 18.55493 ? 152 GLU A O   1 
ATOM   1045 C  CB  . GLU A 1 137 ? -34.70600 -16.58500 -9.33400  1.000 23.48469 ? 152 GLU A CB  1 
ATOM   1046 C  CG  . GLU A 1 137 ? -33.32700 -17.04700 -9.72000  1.000 25.10345 ? 152 GLU A CG  1 
ATOM   1047 C  CD  . GLU A 1 137 ? -32.69800 -17.89600 -8.63400  1.000 33.24461 ? 152 GLU A CD  1 
ATOM   1048 O  OE1 . GLU A 1 137 ? -33.20800 -17.86800 -7.49100  1.000 36.38036 ? 152 GLU A OE1 1 
ATOM   1049 O  OE2 . GLU A 1 137 ? -31.70000 -18.59100 -8.92400  1.000 39.59509 ? 152 GLU A OE2 1 
ATOM   1050 N  N   . ARG A 1 138 ? -37.41200 -14.46800 -9.73100  1.000 17.78287 ? 153 ARG A N   1 
ATOM   1051 C  CA  . ARG A 1 138 ? -38.79700 -14.35100 -9.28800  1.000 18.29018 ? 153 ARG A CA  1 
ATOM   1052 C  C   . ARG A 1 138 ? -39.64300 -13.49700 -10.22000 1.000 19.05945 ? 153 ARG A C   1 
ATOM   1053 O  O   . ARG A 1 138 ? -40.74600 -13.08200 -9.84600  1.000 21.49173 ? 153 ARG A O   1 
ATOM   1054 C  CB  . ARG A 1 138 ? -38.84000 -13.80200 -7.86500  1.000 17.12271 ? 153 ARG A CB  1 
ATOM   1055 C  CG  . ARG A 1 138 ? -38.41500 -14.85100 -6.88500  1.000 20.27576 ? 153 ARG A CG  1 
ATOM   1056 C  CD  . ARG A 1 138 ? -38.06800 -14.30800 -5.53100  1.000 22.87790 ? 153 ARG A CD  1 
ATOM   1057 N  NE  . ARG A 1 138 ? -37.85100 -15.43300 -4.63500  1.000 25.06019 ? 153 ARG A NE  1 
ATOM   1058 C  CZ  . ARG A 1 138 ? -36.72600 -16.13200 -4.57000  1.000 26.66469 ? 153 ARG A CZ  1 
ATOM   1059 N  NH1 . ARG A 1 138 ? -35.66100 -15.79900 -5.28600  1.000 23.86777 ? 153 ARG A NH1 1 
ATOM   1060 N  NH2 . ARG A 1 138 ? -36.66900 -17.19400 -3.77000  1.000 27.19903 ? 153 ARG A NH2 1 
ATOM   1061 N  N   . ARG A 1 139 ? -39.16100 -13.24500 -11.43100 1.000 18.37924 ? 154 ARG A N   1 
ATOM   1062 C  CA  . ARG A 1 139 ? -39.91600 -12.47900 -12.40600 1.000 19.09964 ? 154 ARG A CA  1 
ATOM   1063 C  C   . ARG A 1 139 ? -39.49500 -12.87900 -13.80500 1.000 20.52327 ? 154 ARG A C   1 
ATOM   1064 O  O   . ARG A 1 139 ? -40.07200 -12.41900 -14.78900 1.000 22.92040 ? 154 ARG A O   1 
ATOM   1065 C  CB  . ARG A 1 139 ? -39.69800 -10.98600 -12.20400 1.000 20.99353 ? 154 ARG A CB  1 
ATOM   1066 C  CG  . ARG A 1 139 ? -38.25900 -10.56500 -12.39000 1.000 23.08858 ? 154 ARG A CG  1 
ATOM   1067 C  CD  . ARG A 1 139 ? -38.08300 -9.12400  -11.96800 1.000 28.78020 ? 154 ARG A CD  1 
ATOM   1068 N  NE  . ARG A 1 139 ? -36.78300 -8.59100  -12.34900 1.000 25.91575 ? 154 ARG A NE  1 
ATOM   1069 C  CZ  . ARG A 1 139 ? -36.39300 -7.34700  -12.10300 1.000 38.34442 ? 154 ARG A CZ  1 
ATOM   1070 N  NH1 . ARG A 1 139 ? -37.17500 -6.49000  -11.46300 1.000 38.14038 ? 154 ARG A NH1 1 
ATOM   1071 N  NH2 . ARG A 1 139 ? -35.19100 -6.95100  -12.51200 1.000 37.95522 ? 154 ARG A NH2 1 
ATOM   1072 O  OXT . ARG A 1 139 ? -38.56200 -13.66800 -13.95800 1.000 19.71406 ? 154 ARG A OXT 1 
HETATM 1073 N  N   . TPO B 2 3   ? -6.79700  -15.24700 2.47000   1.000 29.69621 ? 641 TPO B N   1 
HETATM 1074 C  CA  . TPO B 2 3   ? -6.20100  -14.59100 3.60700   1.000 30.23245 ? 641 TPO B CA  1 
HETATM 1075 C  CB  . TPO B 2 3   ? -5.69300  -13.15900 3.29700   1.000 33.24105 ? 641 TPO B CB  1 
HETATM 1076 C  CG2 . TPO B 2 3   ? -5.03800  -12.56700 4.54400   1.000 38.86451 ? 641 TPO B CG2 1 
HETATM 1077 O  OG1 . TPO B 2 3   ? -4.81200  -13.16300 2.19100   1.000 43.13994 ? 641 TPO B OG1 1 
HETATM 1078 P  P   . TPO B 2 3   ? -3.08800  -13.07900 2.29400   1.000 68.71885 ? 641 TPO B P   1 
HETATM 1079 O  O1P . TPO B 2 3   ? -2.77600  -14.17200 3.31700   1.000 55.28973 ? 641 TPO B O1P 1 
HETATM 1080 O  O2P . TPO B 2 3   ? -2.61900  -13.41400 0.87800   1.000 51.09934 ? 641 TPO B O2P 1 
HETATM 1081 O  O3P . TPO B 2 3   ? -2.71200  -11.65500 2.70800   1.000 50.39756 ? 641 TPO B O3P 1 
HETATM 1082 C  C   . TPO B 2 3   ? -7.23100  -14.57300 4.73700   1.000 24.40096 ? 641 TPO B C   1 
HETATM 1083 O  O   . TPO B 2 3   ? -6.88600  -14.93600 5.84600   1.000 35.62854 ? 641 TPO B O   1 
ATOM   1084 N  N   . ILE B 2 4   ? -8.49100  -14.20300 4.48100   1.000 17.80131 ? 642 ILE B N   1 
ATOM   1085 C  CA  . ILE B 2 4   ? -9.43700  -14.16700 5.60900   1.000 15.55293 ? 642 ILE B CA  1 
ATOM   1086 C  C   . ILE B 2 4   ? -9.94000  -15.56100 5.98100   1.000 16.64311 ? 642 ILE B C   1 
ATOM   1087 O  O   . ILE B 2 4   ? -10.24800 -15.81300 7.15300   1.000 14.51255 ? 642 ILE B O   1 
ATOM   1088 C  CB  . ILE B 2 4   ? -10.64000 -13.20800 5.36400   1.000 14.26038 ? 642 ILE B CB  1 
ATOM   1089 C  CG1 . ILE B 2 4   ? -11.30200 -12.85700 6.71300   1.000 14.55275 ? 642 ILE B CG1 1 
ATOM   1090 C  CG2 . ILE B 2 4   ? -11.67500 -13.83300 4.44200   1.000 12.88610 ? 642 ILE B CG2 1 
ATOM   1091 C  CD1 . ILE B 2 4   ? -12.24400 -11.66000 6.66500   1.000 13.53716 ? 642 ILE B CD1 1 
ATOM   1092 N  N   . GLU B 2 5   ? -10.01200 -16.47500 5.01300   1.000 17.17806 ? 643 GLU B N   1 
ATOM   1093 C  CA  . GLU B 2 5   ? -10.46600 -17.84100 5.28600   1.000 14.07041 ? 643 GLU B CA  1 
ATOM   1094 C  C   . GLU B 2 5   ? -9.29500  -18.70200 5.77100   1.000 17.81190 ? 643 GLU B C   1 
ATOM   1095 O  O   . GLU B 2 5   ? -8.87700  -19.68500 5.15400   1.000 20.35208 ? 643 GLU B O   1 
ATOM   1096 C  CB  . GLU B 2 5   ? -11.14400 -18.43800 4.06000   1.000 24.34464 ? 643 GLU B CB  1 
ATOM   1097 C  CG  . GLU B 2 5   ? -12.38800 -17.67400 3.61900   1.000 20.80051 ? 643 GLU B CG  1 
ATOM   1098 C  CD  . GLU B 2 5   ? -13.09900 -18.34300 2.46900   1.000 34.85156 ? 643 GLU B CD  1 
ATOM   1099 O  OE1 . GLU B 2 5   ? -13.08100 -19.59200 2.40700   1.000 41.09232 ? 643 GLU B OE1 1 
ATOM   1100 O  OE2 . GLU B 2 5   ? -13.67100 -17.62200 1.62300   1.000 39.61223 ? 643 GLU B OE2 1 
ATOM   1101 N  N   . GLU B 2 6   ? -8.76000  -18.28100 6.90800   1.000 16.71088 ? 644 GLU B N   1 
ATOM   1102 C  CA  . GLU B 2 6   ? -7.68600  -18.96800 7.60100   1.000 16.87396 ? 644 GLU B CA  1 
ATOM   1103 C  C   . GLU B 2 6   ? -7.99600  -18.93800 9.08500   1.000 14.51107 ? 644 GLU B C   1 
ATOM   1104 O  O   . GLU B 2 6   ? -8.69400  -18.04300 9.56800   1.000 13.33849 ? 644 GLU B O   1 
ATOM   1105 C  CB  . GLU B 2 6   ? -6.32700  -18.30800 7.36000   1.000 21.01663 ? 644 GLU B CB  1 
ATOM   1106 C  CG  . GLU B 2 6   ? -5.55000  -18.83900 6.18500   1.000 26.57385 ? 644 GLU B CG  1 
ATOM   1107 C  CD  . GLU B 2 6   ? -4.16800  -18.22000 6.12200   1.000 37.69151 ? 644 GLU B CD  1 
ATOM   1108 O  OE1 . GLU B 2 6   ? -3.91900  -17.26000 6.88700   1.000 38.08545 ? 644 GLU B OE1 1 
ATOM   1109 O  OE2 . GLU B 2 6   ? -3.33300  -18.69700 5.31800   1.000 40.63696 ? 644 GLU B OE2 1 
ATOM   1110 N  N   . VAL B 2 7   ? -7.44500  -19.90700 9.81100   1.000 13.25139 ? 645 VAL B N   1 
ATOM   1111 C  CA  . VAL B 2 7   ? -7.62000  -19.95300 11.25800  1.000 13.94839 ? 645 VAL B CA  1 
ATOM   1112 C  C   . VAL B 2 7   ? -6.56700  -19.08000 11.92900  1.000 15.08058 ? 645 VAL B C   1 
ATOM   1113 O  O   . VAL B 2 7   ? -5.47600  -18.83600 11.40000  1.000 16.07454 ? 645 VAL B O   1 
ATOM   1114 C  CB  . VAL B 2 7   ? -7.58400  -21.40800 11.78500  1.000 12.40793 ? 645 VAL B CB  1 
ATOM   1115 C  CG1 . VAL B 2 7   ? -8.83700  -22.15200 11.33200  1.000 12.30614 ? 645 VAL B CG1 1 
ATOM   1116 C  CG2 . VAL B 2 7   ? -6.33500  -22.12500 11.31800  1.000 12.00046 ? 645 VAL B CG2 1 
ATOM   1117 N  N   . ASP B 2 8   ? -6.90500  -18.58900 13.11500  1.000 14.33954 ? 646 ASP B N   1 
ATOM   1118 C  CA  . ASP B 2 8   ? -5.97700  -17.77500 13.89200  1.000 16.57002 ? 646 ASP B CA  1 
ATOM   1119 C  C   . ASP B 2 8   ? -5.35500  -18.56200 15.03100  1.000 18.21119 ? 646 ASP B C   1 
ATOM   1120 O  O   . ASP B 2 8   ? -4.44200  -18.07200 15.69700  1.000 17.66988 ? 646 ASP B O   1 
ATOM   1121 C  CB  . ASP B 2 8   ? -6.68900  -16.54600 14.45200  1.000 15.29954 ? 646 ASP B CB  1 
ATOM   1122 C  CG  . ASP B 2 8   ? -7.18800  -15.63400 13.36900  1.000 20.55637 ? 646 ASP B CG  1 
ATOM   1123 O  OD1 . ASP B 2 8   ? -6.36500  -15.18700 12.54000  1.000 23.53010 ? 646 ASP B OD1 1 
ATOM   1124 O  OD2 . ASP B 2 8   ? -8.40100  -15.37300 13.34100  1.000 20.35418 ? 646 ASP B OD2 1 
ATOM   1125 O  OXT . ASP B 2 8   ? -5.74200  -19.69300 15.31600  1.000 14.32365 ? 646 ASP B OXT 1 
HETATM 1126 CL CL  . CL  C 3 .   ? -10.82300 -32.84600 26.62300  1.000 20.54770 ? 201 CL  A CL  1 
HETATM 1127 O  O   . HOH D 4 .   ? -25.54000 -12.83200 21.90800  1.000 18.73639 ? 301 HOH A O   1 
HETATM 1128 O  O   . HOH D 4 .   ? -2.01300  -28.52300 30.27400  1.000 42.46390 ? 302 HOH A O   1 
HETATM 1129 O  O   . HOH D 4 .   ? -26.34800 -25.33700 5.73100   1.000 35.75620 ? 303 HOH A O   1 
HETATM 1130 O  O   . HOH D 4 .   ? -21.14400 -31.44000 7.34900   1.000 24.39416 ? 304 HOH A O   1 
HETATM 1131 O  O   . HOH D 4 .   ? -4.78800  -19.62100 22.67800  1.000 19.71536 ? 305 HOH A O   1 
HETATM 1132 O  O   . HOH D 4 .   ? -26.59500 -4.11500  -5.08300  1.000 42.32005 ? 306 HOH A O   1 
HETATM 1133 O  O   . HOH D 4 .   ? -31.32000 -15.88300 -12.30800 1.000 47.23115 ? 307 HOH A O   1 
HETATM 1134 O  O   . HOH D 4 .   ? -10.76100 -8.39600  17.18900  1.000 20.87906 ? 308 HOH A O   1 
HETATM 1135 O  O   . HOH D 4 .   ? -27.75600 -6.68100  -5.40300  1.000 23.07839 ? 309 HOH A O   1 
HETATM 1136 O  O   . HOH D 4 .   ? -11.22300 -12.17000 18.31800  1.000 18.33451 ? 310 HOH A O   1 
HETATM 1137 O  O   . HOH D 4 .   ? -10.56200 -17.05500 13.67400  1.000 13.96199 ? 311 HOH A O   1 
HETATM 1138 O  O   . HOH D 4 .   ? -10.70200 -8.44600  14.42100  1.000 14.89943 ? 312 HOH A O   1 
HETATM 1139 O  O   . HOH D 4 .   ? -9.78100  -11.99200 -2.76800  1.000 21.09287 ? 313 HOH A O   1 
HETATM 1140 O  O   . HOH D 4 .   ? -24.14500 -8.41300  13.17600  1.000 19.30073 ? 314 HOH A O   1 
HETATM 1141 O  O   . HOH D 4 .   ? -11.10500 -27.84500 1.66700   1.000 24.27848 ? 315 HOH A O   1 
HETATM 1142 O  O   . HOH D 4 .   ? -20.91500 -26.64000 17.80200  1.000 15.48394 ? 316 HOH A O   1 
HETATM 1143 O  O   . HOH D 4 .   ? -25.74500 -15.49300 25.47400  1.000 26.44534 ? 317 HOH A O   1 
HETATM 1144 O  O   . HOH D 4 .   ? -38.34500 -12.84000 -16.79800 1.000 27.60757 ? 318 HOH A O   1 
HETATM 1145 O  O   . HOH D 4 .   ? -12.39600 -32.92100 6.41600   1.000 18.15556 ? 319 HOH A O   1 
HETATM 1146 O  O   . HOH D 4 .   ? 1.42700   -27.40500 19.35900  1.000 26.72152 ? 320 HOH A O   1 
HETATM 1147 O  O   . HOH D 4 .   ? -17.23900 -5.19900  -3.48700  1.000 24.80382 ? 321 HOH A O   1 
HETATM 1148 O  O   . HOH D 4 .   ? -27.78700 -4.43300  3.71400   1.000 25.40412 ? 322 HOH A O   1 
HETATM 1149 O  O   . HOH D 4 .   ? -10.02700 -9.69200  -6.31000  1.000 27.32152 ? 323 HOH A O   1 
HETATM 1150 O  O   . HOH D 4 .   ? -12.95100 -19.65400 24.02300  1.000 14.89352 ? 324 HOH A O   1 
HETATM 1151 O  O   . HOH D 4 .   ? -12.47600 -1.99900  15.64700  1.000 19.57427 ? 325 HOH A O   1 
HETATM 1152 O  O   . HOH D 4 .   ? -17.59200 -9.66000  -11.29300 1.000 39.31427 ? 326 HOH A O   1 
HETATM 1153 O  O   . HOH D 4 .   ? -3.05200  -30.18400 3.43900   1.000 23.98351 ? 327 HOH A O   1 
HETATM 1154 O  O   . HOH D 4 .   ? -7.32400  -6.84400  14.85300  1.000 27.69800 ? 328 HOH A O   1 
HETATM 1155 O  O   . HOH D 4 .   ? -14.93900 -25.44400 31.09200  1.000 16.43778 ? 329 HOH A O   1 
HETATM 1156 O  O   . HOH D 4 .   ? -36.80800 -19.29300 -10.46900 1.000 20.46077 ? 330 HOH A O   1 
HETATM 1157 O  O   . HOH D 4 .   ? -20.23800 -30.10000 16.11400  1.000 20.23231 ? 331 HOH A O   1 
HETATM 1158 O  O   . HOH D 4 .   ? -19.13300 -3.89900  16.62900  1.000 12.54467 ? 332 HOH A O   1 
HETATM 1159 O  O   . HOH D 4 .   ? -10.31600 -33.78300 17.05400  1.000 13.96035 ? 333 HOH A O   1 
HETATM 1160 O  O   . HOH D 4 .   ? -13.46300 1.91400   9.03100   1.000 27.83725 ? 334 HOH A O   1 
HETATM 1161 O  O   . HOH D 4 .   ? -7.19700  -25.89500 4.92200   1.000 25.77099 ? 335 HOH A O   1 
HETATM 1162 O  O   . HOH D 4 .   ? -27.58700 -21.15100 14.81400  1.000 22.21823 ? 336 HOH A O   1 
HETATM 1163 O  O   . HOH D 4 .   ? -16.59300 -31.51000 14.56200  1.000 12.64948 ? 337 HOH A O   1 
HETATM 1164 O  O   . HOH D 4 .   ? -20.72900 -1.78000  -0.25500  1.000 37.15251 ? 338 HOH A O   1 
HETATM 1165 O  O   . HOH D 4 .   ? -19.86200 -13.65400 0.13100   1.000 19.95341 ? 339 HOH A O   1 
HETATM 1166 O  O   . HOH D 4 .   ? -12.33800 -13.61300 16.17800  1.000 16.30626 ? 340 HOH A O   1 
HETATM 1167 O  O   . HOH D 4 .   ? -8.79200  -4.76800  -1.95700  1.000 23.27689 ? 341 HOH A O   1 
HETATM 1168 O  O   . HOH D 4 .   ? -26.62500 -11.68200 -10.44100 1.000 21.52827 ? 342 HOH A O   1 
HETATM 1169 O  O   . HOH D 4 .   ? -6.21100  -19.89500 26.41400  1.000 20.25675 ? 343 HOH A O   1 
HETATM 1170 O  O   . HOH D 4 .   ? -22.09800 -24.25100 17.13700  1.000 15.43340 ? 344 HOH A O   1 
HETATM 1171 O  O   . HOH D 4 .   ? -0.57400  -29.21200 20.32600  1.000 23.43142 ? 345 HOH A O   1 
HETATM 1172 O  O   . HOH D 4 .   ? -31.40100 -10.18200 5.29700   1.000 28.36428 ? 346 HOH A O   1 
HETATM 1173 O  O   . HOH D 4 .   ? -0.59000  -24.96600 14.61100  1.000 15.46991 ? 347 HOH A O   1 
HETATM 1174 O  O   . HOH D 4 .   ? -11.97000 2.17700   1.81700   1.000 30.55134 ? 348 HOH A O   1 
HETATM 1175 O  O   . HOH D 4 .   ? -16.37000 -11.69600 -6.14900  1.000 15.41817 ? 349 HOH A O   1 
HETATM 1176 O  O   . HOH D 4 .   ? -13.89500 -7.52700  -5.69500  1.000 21.12343 ? 350 HOH A O   1 
HETATM 1177 O  O   . HOH D 4 .   ? -38.43800 -10.19400 -8.40000  1.000 23.86914 ? 351 HOH A O   1 
HETATM 1178 O  O   . HOH D 4 .   ? -12.05100 -35.25400 7.86800   1.000 17.21112 ? 352 HOH A O   1 
HETATM 1179 O  O   . HOH D 4 .   ? -19.54800 -16.32800 24.14200  1.000 17.74719 ? 353 HOH A O   1 
HETATM 1180 O  O   . HOH D 4 .   ? -7.95700  -34.46100 4.85500   1.000 23.05691 ? 354 HOH A O   1 
HETATM 1181 O  O   . HOH D 4 .   ? -7.63500  -6.03600  2.91100   1.000 27.12096 ? 355 HOH A O   1 
HETATM 1182 O  O   . HOH D 4 .   ? -6.28100  -10.45200 -2.60600  1.000 31.30905 ? 356 HOH A O   1 
HETATM 1183 O  O   . HOH D 4 .   ? -28.59200 -15.34500 15.32800  1.000 35.87814 ? 357 HOH A O   1 
HETATM 1184 O  O   . HOH D 4 .   ? -35.96800 -12.76500 -15.00900 1.000 25.43953 ? 358 HOH A O   1 
HETATM 1185 O  O   . HOH D 4 .   ? -29.55300 -16.02300 -5.75100  1.000 23.88949 ? 359 HOH A O   1 
HETATM 1186 O  O   . HOH D 4 .   ? -14.21900 -13.62300 -0.56700  1.000 17.04210 ? 360 HOH A O   1 
HETATM 1187 O  O   . HOH D 4 .   ? -4.75400  -27.93800 0.87700   1.000 36.39793 ? 361 HOH A O   1 
HETATM 1188 O  O   . HOH D 4 .   ? -10.38100 -7.81000  2.20400   1.000 13.06182 ? 362 HOH A O   1 
HETATM 1189 O  O   . HOH D 4 .   ? -3.25300  -7.96600  8.57300   1.000 33.38863 ? 363 HOH A O   1 
HETATM 1190 O  O   . HOH D 4 .   ? -21.02100 -4.57400  14.77000  1.000 12.01002 ? 364 HOH A O   1 
HETATM 1191 O  O   . HOH D 4 .   ? -16.36500 -28.80000 18.80800  1.000 14.14706 ? 365 HOH A O   1 
HETATM 1192 O  O   . HOH D 4 .   ? -24.41900 -10.87600 17.73600  1.000 13.81835 ? 366 HOH A O   1 
HETATM 1193 O  O   . HOH D 4 .   ? -23.87000 -12.40300 19.73000  1.000 12.84060 ? 367 HOH A O   1 
HETATM 1194 O  O   . HOH D 4 .   ? -20.10000 -22.83800 3.24100   1.000 28.47117 ? 368 HOH A O   1 
HETATM 1195 O  O   . HOH D 4 .   ? 0.97000   -23.87700 26.68000  1.000 41.24985 ? 369 HOH A O   1 
HETATM 1196 O  O   . HOH D 4 .   ? -24.87400 -18.68000 19.82200  1.000 24.02561 ? 370 HOH A O   1 
HETATM 1197 O  O   . HOH D 4 .   ? -35.43900 -11.84700 -3.92800  1.000 30.27566 ? 371 HOH A O   1 
HETATM 1198 O  O   . HOH D 4 .   ? -14.87700 -28.94500 2.71400   1.000 24.31928 ? 372 HOH A O   1 
HETATM 1199 O  O   . HOH D 4 .   ? -19.32400 0.14600   10.20000  1.000 20.44679 ? 373 HOH A O   1 
HETATM 1200 O  O   . HOH D 4 .   ? -11.00400 -3.39500  4.86400   1.000 22.10905 ? 374 HOH A O   1 
HETATM 1201 O  O   . HOH D 4 .   ? -9.02100  -24.45000 3.83800   1.000 24.13863 ? 375 HOH A O   1 
HETATM 1202 O  O   . HOH D 4 .   ? -3.20700  -22.12400 27.05200  1.000 19.80895 ? 376 HOH A O   1 
HETATM 1203 O  O   . HOH D 4 .   ? -12.14300 -10.47000 23.50900  1.000 32.71875 ? 377 HOH A O   1 
HETATM 1204 O  O   . HOH D 4 .   ? -11.58400 -31.85000 3.31000   1.000 23.15197 ? 378 HOH A O   1 
HETATM 1205 O  O   . HOH D 4 .   ? -5.03800  -23.84300 29.25500  1.000 25.22738 ? 379 HOH A O   1 
HETATM 1206 O  O   . HOH D 4 .   ? -22.37300 -19.07100 1.86700   1.000 31.65665 ? 380 HOH A O   1 
HETATM 1207 O  O   . HOH D 4 .   ? -22.65000 -7.52100  15.21600  1.000 11.83285 ? 381 HOH A O   1 
HETATM 1208 O  O   . HOH D 4 .   ? -26.99900 -25.70500 8.78600   1.000 20.46719 ? 382 HOH A O   1 
HETATM 1209 O  O   . HOH D 4 .   ? 1.68300   -26.11600 15.04900  1.000 20.72702 ? 383 HOH A O   1 
HETATM 1210 O  O   . HOH D 4 .   ? -16.71100 -8.00500  25.04000  1.000 29.09585 ? 384 HOH A O   1 
HETATM 1211 O  O   . HOH D 4 .   ? -11.68000 -12.96400 23.38300  1.000 19.83420 ? 385 HOH A O   1 
HETATM 1212 O  O   . HOH D 4 .   ? -9.72600  -13.94100 20.62400  1.000 16.71409 ? 386 HOH A O   1 
HETATM 1213 O  O   . HOH D 4 .   ? -24.56600 -16.75200 21.67300  1.000 23.79248 ? 387 HOH A O   1 
HETATM 1214 O  O   . HOH D 4 .   ? -29.17000 -14.19200 10.68800  1.000 34.14123 ? 388 HOH A O   1 
HETATM 1215 O  O   . HOH D 4 .   ? -10.82000 -11.11300 13.18500  1.000 16.67971 ? 389 HOH A O   1 
HETATM 1216 O  O   . HOH D 4 .   ? -16.69800 0.88300   14.95400  1.000 25.05225 ? 390 HOH A O   1 
HETATM 1217 O  O   . HOH D 4 .   ? -34.43400 -19.34200 -3.54300  1.000 39.07832 ? 391 HOH A O   1 
HETATM 1218 O  O   . HOH D 4 .   ? -0.98900  -22.30700 15.13900  1.000 22.24234 ? 392 HOH A O   1 
HETATM 1219 O  O   . HOH D 4 .   ? -18.34700 -12.50400 -7.92600  1.000 19.49480 ? 393 HOH A O   1 
HETATM 1220 O  O   . HOH D 4 .   ? -10.92400 -18.65400 31.55200  1.000 32.69562 ? 394 HOH A O   1 
HETATM 1221 O  O   . HOH D 4 .   ? -29.27900 -14.75700 13.32500  1.000 37.76188 ? 395 HOH A O   1 
HETATM 1222 O  O   . HOH D 4 .   ? -19.57200 -4.49200  -4.15500  1.000 27.60086 ? 396 HOH A O   1 
HETATM 1223 O  O   . HOH D 4 .   ? -32.72700 -9.95400  2.15100   1.000 27.27563 ? 397 HOH A O   1 
HETATM 1224 O  O   . HOH D 4 .   ? -28.66700 -9.55700  -15.10700 1.000 26.42615 ? 398 HOH A O   1 
HETATM 1225 O  O   . HOH D 4 .   ? -13.97400 -5.88200  21.73700  1.000 30.42973 ? 399 HOH A O   1 
HETATM 1226 O  O   . HOH D 4 .   ? -5.37900  -17.59600 20.47300  1.000 26.86237 ? 400 HOH A O   1 
HETATM 1227 O  O   . HOH D 4 .   ? -6.09100  -20.53900 29.15700  1.000 34.85768 ? 401 HOH A O   1 
HETATM 1228 O  O   . HOH D 4 .   ? -35.55300 -4.36800  -9.60500  1.000 34.39804 ? 402 HOH A O   1 
HETATM 1229 O  O   . HOH D 4 .   ? -24.77800 -24.66700 17.92000  1.000 18.58477 ? 403 HOH A O   1 
HETATM 1230 O  O   . HOH D 4 .   ? -20.96600 -21.09000 2.13600   1.000 29.57957 ? 404 HOH A O   1 
HETATM 1231 O  O   . HOH D 4 .   ? -17.46500 -30.67200 16.77900  1.000 16.19101 ? 405 HOH A O   1 
HETATM 1232 O  O   . HOH D 4 .   ? -34.10400 -14.52700 -15.25800 1.000 35.09032 ? 406 HOH A O   1 
HETATM 1233 O  O   . HOH D 4 .   ? 0.09600   -8.37100  5.51300   1.000 45.88583 ? 407 HOH A O   1 
HETATM 1234 O  O   . HOH D 4 .   ? -10.74700 -33.25500 19.85500  1.000 17.99468 ? 408 HOH A O   1 
HETATM 1235 O  O   . HOH D 4 .   ? -16.69500 -14.91100 -0.23900  1.000 24.85599 ? 409 HOH A O   1 
HETATM 1236 O  O   . HOH D 4 .   ? -11.00600 -30.25900 1.05200   1.000 23.79240 ? 410 HOH A O   1 
HETATM 1237 O  O   . HOH D 4 .   ? -14.62600 -9.83500  -7.26200  1.000 17.84408 ? 411 HOH A O   1 
HETATM 1238 O  O   . HOH D 4 .   ? -33.53800 -16.38200 -13.48300 1.000 40.30270 ? 412 HOH A O   1 
HETATM 1239 O  O   . HOH D 4 .   ? -9.69500  -4.05800  0.58600   1.000 36.75756 ? 413 HOH A O   1 
HETATM 1240 O  O   . HOH D 4 .   ? -0.93900  -24.75900 11.67700  1.000 19.48279 ? 414 HOH A O   1 
HETATM 1241 O  O   . HOH D 4 .   ? -20.44500 0.96100   6.25800   1.000 37.23646 ? 415 HOH A O   1 
HETATM 1242 O  O   . HOH D 4 .   ? -2.39900  -22.94200 10.80200  1.000 24.44753 ? 416 HOH A O   1 
HETATM 1243 O  O   . HOH D 4 .   ? -5.10300  -8.02500  -3.53800  1.000 40.41346 ? 417 HOH A O   1 
HETATM 1244 O  O   . HOH D 4 .   ? -27.49900 -18.82900 16.64200  1.000 31.60235 ? 418 HOH A O   1 
HETATM 1245 O  O   . HOH D 4 .   ? -10.52900 -2.65000  17.80700  1.000 31.48564 ? 419 HOH A O   1 
HETATM 1246 O  O   . HOH D 4 .   ? -18.72200 2.78200   10.73800  1.000 24.60374 ? 420 HOH A O   1 
HETATM 1247 O  O   . HOH D 4 .   ? -35.98500 -20.74600 -8.25600  1.000 28.17958 ? 421 HOH A O   1 
HETATM 1248 O  O   . HOH D 4 .   ? -22.99400 -12.34900 -12.71400 1.000 22.71108 ? 422 HOH A O   1 
HETATM 1249 O  O   . HOH D 4 .   ? -10.82200 -5.25400  2.97200   1.000 24.04387 ? 423 HOH A O   1 
HETATM 1250 O  O   . HOH D 4 .   ? -14.46300 -5.10900  -5.70000  1.000 27.66917 ? 424 HOH A O   1 
HETATM 1251 O  O   . HOH D 4 .   ? -34.78200 -19.19500 -12.49000 1.000 25.60504 ? 425 HOH A O   1 
HETATM 1252 O  O   . HOH D 4 .   ? -24.97800 -14.03700 -11.09000 1.000 38.78593 ? 426 HOH A O   1 
HETATM 1253 O  O   . HOH D 4 .   ? -23.16100 1.51800   5.88500   1.000 34.98558 ? 427 HOH A O   1 
HETATM 1254 O  O   . HOH D 4 .   ? -3.36800  -19.24500 26.09700  1.000 35.78577 ? 428 HOH A O   1 
HETATM 1255 O  O   . HOH D 4 .   ? -14.84400 -32.05400 5.88800   1.000 14.22532 ? 429 HOH A O   1 
HETATM 1256 O  O   . HOH D 4 .   ? -27.01000 -18.44400 18.91500  1.000 32.59191 ? 430 HOH A O   1 
HETATM 1257 O  O   . HOH D 4 .   ? -11.60900 -4.35200  21.78900  1.000 34.34284 ? 431 HOH A O   1 
HETATM 1258 O  O   . HOH D 4 .   ? -22.87200 -8.46300  17.79100  1.000 12.17344 ? 432 HOH A O   1 
HETATM 1259 O  O   . HOH D 4 .   ? -13.92600 -19.35900 32.24300  1.000 23.68358 ? 433 HOH A O   1 
HETATM 1260 O  O   . HOH D 4 .   ? -14.07500 -31.33600 3.14800   1.000 18.16114 ? 434 HOH A O   1 
HETATM 1261 O  O   . HOH D 4 .   ? -17.15400 -23.66600 30.62800  1.000 27.24087 ? 435 HOH A O   1 
HETATM 1262 O  O   . HOH D 4 .   ? -0.23900  -35.29500 16.85000  1.000 50.80037 ? 436 HOH A O   1 
HETATM 1263 O  O   . HOH D 4 .   ? -24.56100 -10.29900 -11.92300 1.000 23.29618 ? 437 HOH A O   1 
HETATM 1264 O  O   . HOH E 4 .   ? -6.23300  -14.72200 8.06300   1.000 23.78119 ? 701 HOH B O   1 
HETATM 1265 O  O   . HOH E 4 .   ? -4.07800  -15.66900 16.52300  1.000 39.25293 ? 702 HOH B O   1 
HETATM 1266 O  O   . HOH E 4 .   ? -12.79700 -15.15900 0.73600   1.000 21.28063 ? 703 HOH B O   1 
HETATM 1267 O  O   . HOH E 4 .   ? -9.81600  -13.23800 14.50700  1.000 19.48106 ? 704 HOH B O   1 
HETATM 1268 O  O   . HOH E 4 .   ? -5.33400  -21.56800 8.01600   1.000 27.80358 ? 705 HOH B O   1 
HETATM 1269 O  O   . HOH E 4 .   ? -8.16700  -11.42800 12.15000  1.000 31.85385 ? 706 HOH B O   1 
HETATM 1270 O  O   . HOH E 4 .   ? -4.85300  -23.00500 6.09300   1.000 36.23788 ? 707 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . SER A 8   ? 0.53704 0.57239 0.57725 -0.00636 -0.03218 0.02092  23  SER A N   
2    C  CA  . SER A 8   ? 0.49665 0.52533 0.52728 -0.01089 -0.03316 0.01775  23  SER A CA  
3    C  C   . SER A 8   ? 0.44583 0.47950 0.48114 -0.01322 -0.03316 0.01839  23  SER A C   
4    O  O   . SER A 8   ? 0.52400 0.55791 0.56016 -0.01753 -0.03889 0.02108  23  SER A O   
5    C  CB  . SER A 8   ? 0.45795 0.47961 0.48049 -0.01459 -0.03937 0.01881  23  SER A CB  
6    N  N   . PRO A 9   ? 0.36660 0.40316 0.40415 -0.01079 -0.02747 0.01619  24  PRO A N   
7    C  CA  . PRO A 9   ? 0.32362 0.36580 0.36666 -0.01267 -0.02707 0.01749  24  PRO A CA  
8    C  C   . PRO A 9   ? 0.28183 0.31612 0.31534 -0.01736 -0.02967 0.01491  24  PRO A C   
9    O  O   . PRO A 9   ? 0.33472 0.36037 0.35727 -0.01722 -0.02824 0.01091  24  PRO A O   
10   C  CB  . PRO A 9   ? 0.27453 0.31951 0.31954 -0.00806 -0.02005 0.01523  24  PRO A CB  
11   C  CG  . PRO A 9   ? 0.32126 0.35803 0.35759 -0.00598 -0.01792 0.01115  24  PRO A CG  
12   C  CD  . PRO A 9   ? 0.36277 0.39665 0.39737 -0.00657 -0.02196 0.01285  24  PRO A CD  
13   N  N   . SER A 10  ? 0.23605 0.27330 0.27384 -0.02126 -0.03354 0.01789  25  SER A N   
14   C  CA  . SER A 10  ? 0.22573 0.25390 0.25346 -0.02511 -0.03617 0.01544  25  SER A CA  
15   C  C   . SER A 10  ? 0.20298 0.23095 0.22861 -0.02295 -0.02975 0.01164  25  SER A C   
16   O  O   . SER A 10  ? 0.19270 0.22792 0.22531 -0.01932 -0.02421 0.01148  25  SER A O   
17   C  CB  . SER A 10  ? 0.27290 0.30319 0.30589 -0.03074 -0.04343 0.02038  25  SER A CB  
18   O  OG  . SER A 10  ? 0.22121 0.26371 0.26767 -0.03030 -0.04036 0.02394  25  SER A OG  
19   N  N   . ALA A 11  ? 0.20958 0.22793 0.22418 -0.02482 -0.03082 0.00864  26  ALA A N   
20   C  CA  . ALA A 11  ? 0.18660 0.20466 0.19938 -0.02313 -0.02559 0.00560  26  ALA A CA  
21   C  C   . ALA A 11  ? 0.18122 0.20865 0.20525 -0.02406 -0.02455 0.00857  26  ALA A C   
22   O  O   . ALA A 11  ? 0.15246 0.18456 0.17996 -0.02096 -0.01882 0.00721  26  ALA A O   
23   C  CB  . ALA A 11  ? 0.19433 0.20012 0.19325 -0.02438 -0.02732 0.00269  26  ALA A CB  
24   N  N   . GLN A 12  ? 0.17542 0.20568 0.20515 -0.02848 -0.03037 0.01329  27  GLN A N   
25   C  CA  . GLN A 12  ? 0.17229 0.21328 0.21414 -0.02945 -0.02907 0.01769  27  GLN A CA  
26   C  C   . GLN A 12  ? 0.17389 0.22727 0.22707 -0.02434 -0.02339 0.02012  27  GLN A C   
27   O  O   . GLN A 12  ? 0.16028 0.22003 0.21834 -0.02147 -0.01790 0.02070  27  GLN A O   
28   C  CB  . GLN A 12  ? 0.20744 0.24979 0.25461 -0.03611 -0.03755 0.02383  27  GLN A CB  
29   C  CG  . GLN A 12  ? 0.21081 0.26796 0.27421 -0.03734 -0.03639 0.03102  27  GLN A CG  
30   C  CD  . GLN A 12  ? 0.30299 0.36008 0.36509 -0.03698 -0.03202 0.02951  27  GLN A CD  
31   O  OE1 . GLN A 12  ? 0.34931 0.39431 0.39857 -0.03724 -0.03187 0.02371  27  GLN A OE1 
32   N  NE2 . GLN A 12  ? 0.29496 0.36598 0.37039 -0.03582 -0.02810 0.03529  27  GLN A NE2 
33   N  N   . GLU A 13  ? 0.15339 0.20896 0.20930 -0.02253 -0.02455 0.02150  28  GLU A N   
34   C  CA  . GLU A 13  ? 0.15917 0.22384 0.22323 -0.01641 -0.01907 0.02335  28  GLU A CA  
35   C  C   . GLU A 13  ? 0.14511 0.20477 0.20162 -0.01139 -0.01249 0.01744  28  GLU A C   
36   O  O   . GLU A 13  ? 0.14779 0.21269 0.20808 -0.00636 -0.00700 0.01818  28  GLU A O   
37   C  CB  . GLU A 13  ? 0.16625 0.23216 0.23307 -0.01546 -0.02227 0.02563  28  GLU A CB  
38   C  CG  . GLU A 13  ? 0.24626 0.32200 0.32566 -0.01895 -0.02792 0.03383  28  GLU A CG  
39   C  CD  . GLU A 13  ? 0.30860 0.38421 0.38960 -0.01857 -0.03222 0.03601  28  GLU A CD  
40   O  OE1 . GLU A 13  ? 0.33279 0.39718 0.40190 -0.01849 -0.03341 0.03079  28  GLU A OE1 
41   O  OE2 . GLU A 13  ? 0.43604 0.52354 0.53081 -0.01820 -0.03428 0.04364  28  GLU A OE2 
42   N  N   . LEU A 14  ? 0.13311 0.18229 0.17845 -0.01254 -0.01312 0.01208  29  LEU A N   
43   C  CA  . LEU A 14  ? 0.10763 0.15237 0.14691 -0.00899 -0.00825 0.00752  29  LEU A CA  
44   C  C   . LEU A 14  ? 0.11902 0.16482 0.15793 -0.00892 -0.00510 0.00641  29  LEU A C   
45   O  O   . LEU A 14  ? 0.09470 0.14038 0.13231 -0.00508 -0.00087 0.00477  29  LEU A O   
46   C  CB  . LEU A 14  ? 0.11316 0.14886 0.14287 -0.01035 -0.00956 0.00382  29  LEU A CB  
47   C  CG  . LEU A 14  ? 0.13949 0.17357 0.16866 -0.00930 -0.01149 0.00464  29  LEU A CG  
48   C  CD1 . LEU A 14  ? 0.17633 0.20261 0.19633 -0.01135 -0.01320 0.00259  29  LEU A CD1 
49   C  CD2 . LEU A 14  ? 0.18835 0.22246 0.21841 -0.00468 -0.00826 0.00383  29  LEU A CD2 
50   N  N   . LYS A 15  ? 0.11065 0.15596 0.14935 -0.01313 -0.00762 0.00731  30  LYS A N   
51   C  CA  . LYS A 15  ? 0.12644 0.17335 0.16559 -0.01309 -0.00480 0.00702  30  LYS A CA  
52   C  C   . LYS A 15  ? 0.13044 0.18730 0.17860 -0.00997 -0.00124 0.01122  30  LYS A C   
53   O  O   . LYS A 15  ? 0.11614 0.17337 0.16249 -0.00667 0.00335  0.00991  30  LYS A O   
54   C  CB  . LYS A 15  ? 0.13942 0.18296 0.17642 -0.01824 -0.00887 0.00784  30  LYS A CB  
55   C  CG  . LYS A 15  ? 0.12020 0.16350 0.15582 -0.01809 -0.00595 0.00684  30  LYS A CG  
56   C  CD  . LYS A 15  ? 0.14859 0.19055 0.18496 -0.02314 -0.01017 0.00960  30  LYS A CD  
57   C  CE  . LYS A 15  ? 0.19103 0.24395 0.23982 -0.02522 -0.01173 0.01673  30  LYS A CE  
58   N  NZ  . LYS A 15  ? 0.24203 0.29423 0.29270 -0.03084 -0.01600 0.02046  30  LYS A NZ  
59   N  N   . GLU A 16  ? 0.11861 0.18368 0.17626 -0.01057 -0.00319 0.01682  31  GLU A N   
60   C  CA  . GLU A 16  ? 0.12167 0.19814 0.18907 -0.00647 0.00117  0.02226  31  GLU A CA  
61   C  C   . GLU A 16  ? 0.11668 0.19147 0.18009 0.00149  0.00684  0.01977  31  GLU A C   
62   O  O   . GLU A 16  ? 0.11911 0.19744 0.18295 0.00658  0.01248  0.02108  31  GLU A O   
63   C  CB  . GLU A 16  ? 0.12672 0.21348 0.20665 -0.00886 -0.00269 0.02988  31  GLU A CB  
64   C  CG  . GLU A 16  ? 0.16850 0.25581 0.25201 -0.01730 -0.00957 0.03344  31  GLU A CG  
65   C  CD  . GLU A 16  ? 0.17558 0.27103 0.27052 -0.02108 -0.01576 0.04098  31  GLU A CD  
66   O  OE1 . GLU A 16  ? 0.22276 0.32189 0.32138 -0.01725 -0.01510 0.04226  31  GLU A OE1 
67   O  OE2 . GLU A 16  ? 0.26300 0.36045 0.36300 -0.02821 -0.02201 0.04594  31  GLU A OE2 
68   N  N   . GLN A 17  ? 0.08149 0.14954 0.13961 0.00281  0.00521  0.01634  32  GLN A N   
69   C  CA  . GLN A 17  ? 0.11639 0.17906 0.16798 0.00969  0.00924  0.01337  32  GLN A CA  
70   C  C   . GLN A 17  ? 0.11915 0.17347 0.16074 0.01044  0.01156  0.00831  32  GLN A C   
71   O  O   . GLN A 17  ? 0.13255 0.18445 0.16943 0.01636  0.01587  0.00760  32  GLN A O   
72   C  CB  . GLN A 17  ? 0.13664 0.19275 0.18430 0.00969  0.00606  0.01105  32  GLN A CB  
73   C  CG  . GLN A 17  ? 0.17012 0.21811 0.20963 0.01608  0.00883  0.00806  32  GLN A CG  
74   C  CD  . GLN A 17  ? 0.21871 0.25984 0.25447 0.01556  0.00530  0.00636  32  GLN A CD  
75   O  OE1 . GLN A 17  ? 0.27127 0.31424 0.31032 0.01089  0.00131  0.00744  32  GLN A OE1 
76   N  NE2 . GLN A 17  ? 0.29228 0.32407 0.31979 0.02034  0.00636  0.00384  32  GLN A NE2 
77   N  N   . GLY A 18  ? 0.09360 0.14285 0.13104 0.00496  0.00864  0.00506  33  GLY A N   
78   C  CA  . GLY A 18  ? 0.10746 0.15034 0.13723 0.00517  0.01022  0.00129  33  GLY A CA  
79   C  C   . GLY A 18  ? 0.10734 0.15477 0.13863 0.00732  0.01409  0.00332  33  GLY A C   
80   O  O   . GLY A 18  ? 0.10660 0.14878 0.13067 0.01098  0.01680  0.00116  33  GLY A O   
81   N  N   . ASN A 19  ? 0.09734 0.15397 0.13751 0.00479  0.01391  0.00798  34  ASN A N   
82   C  CA  . ASN A 19  ? 0.10292 0.16528 0.14572 0.00644  0.01781  0.01117  34  ASN A CA  
83   C  C   . ASN A 19  ? 0.11860 0.18413 0.16102 0.01475  0.02366  0.01355  34  ASN A C   
84   O  O   . ASN A 19  ? 0.10328 0.16727 0.14034 0.01872  0.02805  0.01340  34  ASN A O   
85   C  CB  . ASN A 19  ? 0.09782 0.16970 0.15145 0.00120  0.01539  0.01702  34  ASN A CB  
86   C  CG  . ASN A 19  ? 0.10967 0.17554 0.16011 -0.00586 0.01017  0.01446  34  ASN A CG  
87   O  OD1 . ASN A 19  ? 0.12079 0.17738 0.16239 -0.00636 0.00920  0.00881  34  ASN A OD1 
88   N  ND2 . ASN A 19  ? 0.12463 0.19548 0.18218 -0.01120 0.00648  0.01923  34  ASN A ND2 
89   N  N   . ARG A 20  ? 0.11587 0.18520 0.16295 0.01815  0.02398  0.01599  35  ARG A N   
90   C  CA  . ARG A 20  ? 0.11863 0.18930 0.16348 0.02774  0.03005  0.01810  35  ARG A CA  
91   C  C   . ARG A 20  ? 0.13586 0.19088 0.16408 0.03235  0.03118  0.01139  35  ARG A C   
92   O  O   . ARG A 20  ? 0.12519 0.17684 0.14557 0.03915  0.03636  0.01145  35  ARG A O   
93   C  CB  . ARG A 20  ? 0.13069 0.20745 0.18344 0.03065  0.02953  0.02188  35  ARG A CB  
94   C  CG  . ARG A 20  ? 0.11865 0.21232 0.18889 0.02744  0.02864  0.03056  35  ARG A CG  
95   C  CD  . ARG A 20  ? 0.14437 0.24523 0.22258 0.03269  0.02954  0.03542  35  ARG A CD  
96   N  NE  . ARG A 20  ? 0.13425 0.22639 0.20822 0.03005  0.02387  0.03095  35  ARG A NE  
97   C  CZ  . ARG A 20  ? 0.13988 0.23377 0.21961 0.02179  0.01680  0.03167  35  ARG A CZ  
98   N  NH1 . ARG A 20  ? 0.15043 0.25262 0.23946 0.01466  0.01338  0.03613  35  ARG A NH1 
99   N  NH2 . ARG A 20  ? 0.15577 0.24157 0.23053 0.02065  0.01268  0.02801  35  ARG A NH2 
100  N  N   . LEU A 21  ? 0.14523 0.18996 0.16728 0.02849  0.02597  0.00604  36  LEU A N   
101  C  CA  . LEU A 21  ? 0.12952 0.15890 0.13658 0.03086  0.02507  0.00041  36  LEU A CA  
102  C  C   . LEU A 21  ? 0.14295 0.16884 0.14384 0.02953  0.02610  -0.00139 36  LEU A C   
103  O  O   . LEU A 21  ? 0.14257 0.15762 0.13057 0.03434  0.02752  -0.00398 36  LEU A O   
104  C  CB  . LEU A 21  ? 0.12957 0.15157 0.13434 0.02542  0.01897  -0.00324 36  LEU A CB  
105  C  CG  . LEU A 21  ? 0.13336 0.15466 0.14017 0.02778  0.01764  -0.00225 36  LEU A CG  
106  C  CD1 . LEU A 21  ? 0.13971 0.15821 0.14793 0.02102  0.01208  -0.00407 36  LEU A CD1 
107  C  CD2 . LEU A 21  ? 0.14411 0.15280 0.13825 0.03560  0.01905  -0.00431 36  LEU A CD2 
108  N  N   . PHE A 22  ? 0.11270 0.14619 0.12132 0.02322  0.02494  -0.00003 37  PHE A N   
109  C  CA  . PHE A 22  ? 0.14119 0.17217 0.14480 0.02204  0.02595  -0.00114 37  PHE A CA  
110  C  C   . PHE A 22  ? 0.16357 0.19743 0.16426 0.02910  0.03243  0.00204  37  PHE A C   
111  O  O   . PHE A 22  ? 0.17303 0.19789 0.16177 0.03227  0.03387  -0.00033 37  PHE A O   
112  C  CB  . PHE A 22  ? 0.13233 0.17031 0.14454 0.01461  0.02349  0.00019  37  PHE A CB  
113  C  CG  . PHE A 22  ? 0.13524 0.16936 0.14214 0.01264  0.02339  -0.00146 37  PHE A CG  
114  C  CD1 . PHE A 22  ? 0.15833 0.18427 0.15944 0.00943  0.01949  -0.00558 37  PHE A CD1 
115  C  CD2 . PHE A 22  ? 0.15540 0.19484 0.16381 0.01409  0.02721  0.00194  37  PHE A CD2 
116  C  CE1 . PHE A 22  ? 0.15346 0.17624 0.15020 0.00788  0.01913  -0.00659 37  PHE A CE1 
117  C  CE2 . PHE A 22  ? 0.16002 0.19543 0.16305 0.01238  0.02693  0.00060  37  PHE A CE2 
118  C  CZ  . PHE A 22  ? 0.16979 0.19663 0.16688 0.00939  0.02271  -0.00387 37  PHE A CZ  
119  N  N   . VAL A 23  ? 0.13464 0.18112 0.14596 0.03187  0.03636  0.00805  38  VAL A N   
120  C  CA  . VAL A 23  ? 0.15581 0.20686 0.16524 0.03996  0.04385  0.01245  38  VAL A CA  
121  C  C   . VAL A 23  ? 0.18729 0.22445 0.18018 0.04945  0.04665  0.00886  38  VAL A C   
122  O  O   . VAL A 23  ? 0.19788 0.22927 0.17930 0.05593  0.05143  0.00882  38  VAL A O   
123  C  CB  . VAL A 23  ? 0.15949 0.22851 0.18590 0.04105  0.04708  0.02097  38  VAL A CB  
124  C  CG1 . VAL A 23  ? 0.16508 0.24026 0.19011 0.05125  0.05622  0.02670  38  VAL A CG1 
125  C  CG2 . VAL A 23  ? 0.16835 0.24777 0.20797 0.03125  0.04327  0.02461  38  VAL A CG2 
126  N  N   . GLY A 24  ? 0.17107 0.20090 0.16077 0.05048  0.04332  0.00577  39  GLY A N   
127  C  CA  . GLY A 24  ? 0.18578 0.19882 0.15775 0.05869  0.04416  0.00179  39  GLY A CA  
128  C  C   . GLY A 24  ? 0.20829 0.20296 0.16377 0.05586  0.03888  -0.00485 39  GLY A C   
129  O  O   . GLY A 24  ? 0.22248 0.19995 0.16114 0.06153  0.03766  -0.00850 39  GLY A O   
130  N  N   . ARG A 25  ? 0.19796 0.19523 0.15752 0.04737  0.03527  -0.00606 40  ARG A N   
131  C  CA  . ARG A 25  ? 0.20209 0.18470 0.14920 0.04353  0.02956  -0.01106 40  ARG A CA  
132  C  C   . ARG A 25  ? 0.19605 0.16779 0.13897 0.04006  0.02245  -0.01464 40  ARG A C   
133  O  O   . ARG A 25  ? 0.24632 0.20194 0.17522 0.03952  0.01747  -0.01817 40  ARG A O   
134  C  CB  . ARG A 25  ? 0.24293 0.21213 0.17117 0.05099  0.03239  -0.01260 40  ARG A CB  
135  C  CG  . ARG A 25  ? 0.25305 0.23345 0.18506 0.05530  0.04035  -0.00805 40  ARG A CG  
136  C  CD  . ARG A 25  ? 0.29611 0.26235 0.20862 0.06027  0.04172  -0.01013 40  ARG A CD  
137  N  NE  . ARG A 25  ? 0.32596 0.27292 0.21729 0.06968  0.04228  -0.01320 40  ARG A NE  
138  C  CZ  . ARG A 25  ? 0.33010 0.27673 0.21446 0.08152  0.05070  -0.01047 40  ARG A CZ  
139  N  NH1 . ARG A 25  ? 0.36169 0.32865 0.26161 0.08428  0.05877  -0.00348 40  ARG A NH1 
140  N  NH2 . ARG A 25  ? 0.37342 0.30035 0.23888 0.08791  0.04850  -0.01309 40  ARG A NH2 
141  N  N   . LYS A 26  ? 0.17315 0.15347 0.12827 0.03708  0.02129  -0.01318 41  LYS A N   
142  C  CA  . LYS A 26  ? 0.16642 0.13890 0.11997 0.03309  0.01490  -0.01543 41  LYS A CA  
143  C  C   . LYS A 26  ? 0.14722 0.12785 0.11192 0.02359  0.01106  -0.01513 41  LYS A C   
144  O  O   . LYS A 26  ? 0.15184 0.14218 0.12794 0.02028  0.01081  -0.01339 41  LYS A O   
145  C  CB  . LYS A 26  ? 0.19465 0.16999 0.15244 0.03721  0.01653  -0.01378 41  LYS A CB  
146  C  CG  . LYS A 26  ? 0.23977 0.20628 0.18530 0.04836  0.02115  -0.01377 41  LYS A CG  
147  C  CD  . LYS A 26  ? 0.28514 0.26100 0.23949 0.05379  0.02522  -0.01010 41  LYS A CD  
148  C  CE  . LYS A 26  ? 0.34702 0.32201 0.29409 0.06610  0.03326  -0.00777 41  LYS A CE  
149  N  NZ  . LYS A 26  ? 0.29436 0.28076 0.25197 0.07233  0.03781  -0.00279 41  LYS A NZ  
150  N  N   . TYR A 27  ? 0.14410 0.11985 0.10436 0.01972  0.00797  -0.01663 42  TYR A N   
151  C  CA  . TYR A 27  ? 0.15194 0.13665 0.12239 0.01263  0.00618  -0.01571 42  TYR A CA  
152  C  C   . TYR A 27  ? 0.11818 0.10309 0.09366 0.00739  0.00156  -0.01544 42  TYR A C   
153  O  O   . TYR A 27  ? 0.14033 0.13510 0.12577 0.00400  0.00230  -0.01396 42  TYR A O   
154  C  CB  . TYR A 27  ? 0.14142 0.12207 0.10652 0.01080  0.00467  -0.01659 42  TYR A CB  
155  C  CG  . TYR A 27  ? 0.16612 0.14752 0.12641 0.01588  0.00984  -0.01621 42  TYR A CG  
156  C  CD1 . TYR A 27  ? 0.16821 0.16241 0.13817 0.01684  0.01508  -0.01348 42  TYR A CD1 
157  C  CD2 . TYR A 27  ? 0.17939 0.14810 0.12486 0.01953  0.00909  -0.01801 42  TYR A CD2 
158  C  CE1 . TYR A 27  ? 0.17016 0.16654 0.13696 0.02131  0.02018  -0.01184 42  TYR A CE1 
159  C  CE2 . TYR A 27  ? 0.21737 0.18693 0.15756 0.02489  0.01467  -0.01708 42  TYR A CE2 
160  C  CZ  . TYR A 27  ? 0.24205 0.22648 0.19387 0.02574  0.02056  -0.01364 42  TYR A CZ  
161  O  OH  . TYR A 27  ? 0.23010 0.21655 0.17761 0.03089  0.02639  -0.01154 42  TYR A OH  
162  N  N   . PRO A 28  ? 0.16018 0.13398 0.12854 0.00645  -0.00343 -0.01636 43  PRO A N   
163  C  CA  . PRO A 28  ? 0.16148 0.13755 0.13620 0.00156  -0.00702 -0.01482 43  PRO A CA  
164  C  C   . PRO A 28  ? 0.15127 0.13394 0.13237 0.00310  -0.00440 -0.01387 43  PRO A C   
165  O  O   . PRO A 28  ? 0.12428 0.11423 0.11334 -0.00058 -0.00478 -0.01216 43  PRO A O   
166  C  CB  . PRO A 28  ? 0.18508 0.14612 0.14952 0.00070  -0.01331 -0.01550 43  PRO A CB  
167  C  CG  . PRO A 28  ? 0.21182 0.16343 0.16527 0.00276  -0.01441 -0.01743 43  PRO A CG  
168  C  CD  . PRO A 28  ? 0.15799 0.11579 0.11162 0.00872  -0.00703 -0.01837 43  PRO A CD  
169  N  N   . GLU A 29  ? 0.14437 0.12438 0.12152 0.00902  -0.00167 -0.01455 44  GLU A N   
170  C  CA  . GLU A 29  ? 0.13272 0.11960 0.11663 0.01069  0.00040  -0.01299 44  GLU A CA  
171  C  C   . GLU A 29  ? 0.12457 0.12507 0.11898 0.00886  0.00359  -0.01120 44  GLU A C   
172  O  O   . GLU A 29  ? 0.11775 0.12411 0.11879 0.00619  0.00281  -0.00976 44  GLU A O   
173  C  CB  . GLU A 29  ? 0.18336 0.16467 0.16088 0.01849  0.00292  -0.01331 44  GLU A CB  
174  C  CG  . GLU A 29  ? 0.23423 0.19867 0.19901 0.02070  -0.00128 -0.01526 44  GLU A CG  
175  C  CD  . GLU A 29  ? 0.25941 0.21007 0.21037 0.02194  -0.00350 -0.01782 44  GLU A CD  
176  O  OE1 . GLU A 29  ? 0.23087 0.18533 0.18185 0.02177  -0.00114 -0.01816 44  GLU A OE1 
177  O  OE2 . GLU A 29  ? 0.34469 0.27906 0.28350 0.02288  -0.00842 -0.01941 44  GLU A OE2 
178  N  N   . ALA A 30  ? 0.12579 0.13010 0.12067 0.00993  0.00656  -0.01112 45  ALA A N   
179  C  CA  . ALA A 30  ? 0.09348 0.10858 0.09718 0.00732  0.00833  -0.00921 45  ALA A CA  
180  C  C   . ALA A 30  ? 0.10318 0.11956 0.10944 0.00172  0.00571  -0.00962 45  ALA A C   
181  O  O   . ALA A 30  ? 0.09938 0.12093 0.11080 -0.00061 0.00524  -0.00833 45  ALA A O   
182  C  CB  . ALA A 30  ? 0.10436 0.12225 0.10737 0.00916  0.01166  -0.00862 45  ALA A CB  
183  N  N   . ALA A 31  ? 0.10684 0.11816 0.10900 -0.00015 0.00385  -0.01095 46  ALA A N   
184  C  CA  . ALA A 31  ? 0.10495 0.11860 0.10996 -0.00417 0.00243  -0.01039 46  ALA A CA  
185  C  C   . ALA A 31  ? 0.09677 0.11125 0.10402 -0.00555 0.00104  -0.00928 46  ALA A C   
186  O  O   . ALA A 31  ? 0.10102 0.11914 0.11071 -0.00720 0.00148  -0.00841 46  ALA A O   
187  C  CB  . ALA A 31  ? 0.09955 0.10891 0.10154 -0.00586 0.00019  -0.01062 46  ALA A CB  
188  N  N   . ALA A 32  ? 0.11856 0.12823 0.12344 -0.00456 -0.00078 -0.00927 47  ALA A N   
189  C  CA  . ALA A 32  ? 0.09841 0.10860 0.10507 -0.00585 -0.00216 -0.00785 47  ALA A CA  
190  C  C   . ALA A 32  ? 0.10856 0.12363 0.11849 -0.00495 -0.00088 -0.00726 47  ALA A C   
191  O  O   . ALA A 32  ? 0.12781 0.14453 0.13876 -0.00667 -0.00155 -0.00612 47  ALA A O   
192  C  CB  . ALA A 32  ? 0.12949 0.13206 0.13217 -0.00489 -0.00491 -0.00787 47  ALA A CB  
193  N  N   A CYS A 33  ? 0.11409 0.13144 0.12551 -0.00219 0.00071  -0.00738 48  CYS A N   
194  N  N   B CYS A 33  ? 0.10531 0.12276 0.11676 -0.00228 0.00075  -0.00739 48  CYS A N   
195  C  CA  A CYS A 33  ? 0.11002 0.13305 0.12621 -0.00236 0.00081  -0.00563 48  CYS A CA  
196  C  CA  B CYS A 33  ? 0.11414 0.13710 0.13028 -0.00239 0.00078  -0.00565 48  CYS A CA  
197  C  C   A CYS A 33  ? 0.10783 0.13314 0.12464 -0.00567 0.00040  -0.00550 48  CYS A C   
198  C  C   B CYS A 33  ? 0.09938 0.12490 0.11639 -0.00562 0.00043  -0.00544 48  CYS A C   
199  O  O   A CYS A 33  ? 0.09463 0.12033 0.11165 -0.00744 -0.00150 -0.00448 48  CYS A O   
200  O  O   B CYS A 33  ? 0.09280 0.11912 0.11046 -0.00736 -0.00149 -0.00430 48  CYS A O   
201  C  CB  A CYS A 33  ? 0.11929 0.14664 0.13895 0.00114  0.00307  -0.00425 48  CYS A CB  
202  C  CB  B CYS A 33  ? 0.11827 0.14519 0.13770 0.00132  0.00295  -0.00428 48  CYS A CB  
203  S  SG  A CYS A 33  ? 0.13655 0.16249 0.15631 0.00668  0.00371  -0.00300 48  CYS A SG  
204  S  SG  B CYS A 33  ? 0.14568 0.17853 0.17192 0.00217  0.00164  -0.00071 48  CYS A SG  
205  N  N   . TYR A 34  ? 0.10711 0.13240 0.12273 -0.00623 0.00181  -0.00655 49  TYR A N   
206  C  CA  . TYR A 34  ? 0.08984 0.11514 0.10420 -0.00857 0.00137  -0.00663 49  TYR A CA  
207  C  C   . TYR A 34  ? 0.09135 0.11353 0.10185 -0.00942 0.00075  -0.00684 49  TYR A C   
208  O  O   . TYR A 34  ? 0.10294 0.12306 0.11016 -0.01038 -0.00025 -0.00664 49  TYR A O   
209  C  CB  . TYR A 34  ? 0.09367 0.11909 0.10725 -0.00853 0.00303  -0.00753 49  TYR A CB  
210  C  CG  . TYR A 34  ? 0.08420 0.11315 0.10100 -0.00738 0.00438  -0.00654 49  TYR A CG  
211  C  CD1 . TYR A 34  ? 0.08960 0.12298 0.11115 -0.00823 0.00351  -0.00395 49  TYR A CD1 
212  C  CD2 . TYR A 34  ? 0.08977 0.11776 0.10478 -0.00542 0.00634  -0.00745 49  TYR A CD2 
213  C  CE1 . TYR A 34  ? 0.09238 0.13107 0.11834 -0.00680 0.00556  -0.00159 49  TYR A CE1 
214  C  CE2 . TYR A 34  ? 0.10184 0.13314 0.11874 -0.00345 0.00856  -0.00601 49  TYR A CE2 
215  C  CZ  . TYR A 34  ? 0.09245 0.13000 0.11553 -0.00394 0.00867  -0.00277 49  TYR A CZ  
216  O  OH  . TYR A 34  ? 0.09476 0.13747 0.12099 -0.00157 0.01168  -0.00004 49  TYR A OH  
217  N  N   . GLY A 35  ? 0.10397 0.12512 0.11409 -0.00897 0.00110  -0.00673 50  GLY A N   
218  C  CA  . GLY A 35  ? 0.09066 0.11070 0.09845 -0.00947 0.00120  -0.00551 50  GLY A CA  
219  C  C   . GLY A 35  ? 0.10513 0.12372 0.11105 -0.00969 -0.00038 -0.00475 50  GLY A C   
220  O  O   . GLY A 35  ? 0.09657 0.11306 0.09780 -0.00956 -0.00003 -0.00407 50  GLY A O   
221  N  N   . ARG A 36  ? 0.10603 0.12518 0.11474 -0.00941 -0.00205 -0.00460 51  ARG A N   
222  C  CA  . ARG A 36  ? 0.10277 0.12087 0.11042 -0.00981 -0.00432 -0.00345 51  ARG A CA  
223  C  C   . ARG A 36  ? 0.12452 0.14175 0.12999 -0.01110 -0.00604 -0.00344 51  ARG A C   
224  O  O   . ARG A 36  ? 0.12417 0.13751 0.12433 -0.01188 -0.00812 -0.00283 51  ARG A O   
225  C  CB  . ARG A 36  ? 0.13078 0.15042 0.14284 -0.00844 -0.00555 -0.00270 51  ARG A CB  
226  C  CG  . ARG A 36  ? 0.15381 0.17062 0.16530 -0.00736 -0.00542 -0.00272 51  ARG A CG  
227  C  CD  . ARG A 36  ? 0.15210 0.16848 0.16584 -0.00468 -0.00647 -0.00206 51  ARG A CD  
228  N  NE  . ARG A 36  ? 0.22779 0.24503 0.24255 -0.00507 -0.00878 -0.00015 51  ARG A NE  
229  C  CZ  . ARG A 36  ? 0.22922 0.24813 0.24754 -0.00249 -0.00977 0.00138  51  ARG A CZ  
230  N  NH1 . ARG A 36  ? 0.29115 0.31100 0.31166 0.00152  -0.00780 0.00118  51  ARG A NH1 
231  N  NH2 . ARG A 36  ? 0.24716 0.26654 0.26626 -0.00337 -0.01264 0.00347  51  ARG A NH2 
232  N  N   . ALA A 37  ? 0.09378 0.11342 0.10227 -0.01155 -0.00577 -0.00383 52  ALA A N   
233  C  CA  . ALA A 37  ? 0.11382 0.13123 0.11987 -0.01373 -0.00860 -0.00334 52  ALA A CA  
234  C  C   . ALA A 37  ? 0.13232 0.14240 0.12835 -0.01352 -0.00821 -0.00485 52  ALA A C   
235  O  O   . ALA A 37  ? 0.12302 0.12648 0.11172 -0.01473 -0.01160 -0.00468 52  ALA A O   
236  C  CB  . ALA A 37  ? 0.11018 0.13202 0.12190 -0.01447 -0.00809 -0.00269 52  ALA A CB  
237  N  N   . ILE A 38  ? 0.10743 0.11798 0.10230 -0.01157 -0.00425 -0.00597 53  ILE A N   
238  C  CA  . ILE A 38  ? 0.12196 0.12694 0.10797 -0.00971 -0.00238 -0.00663 53  ILE A CA  
239  C  C   . ILE A 38  ? 0.13686 0.13780 0.11610 -0.00853 -0.00254 -0.00569 53  ILE A C   
240  O  O   . ILE A 38  ? 0.14748 0.14025 0.11556 -0.00701 -0.00294 -0.00615 53  ILE A O   
241  C  CB  . ILE A 38  ? 0.12769 0.13687 0.11709 -0.00792 0.00178  -0.00658 53  ILE A CB  
242  C  CG1 . ILE A 38  ? 0.13233 0.14310 0.12519 -0.00879 0.00170  -0.00769 53  ILE A CG1 
243  C  CG2 . ILE A 38  ? 0.12681 0.13296 0.10903 -0.00462 0.00510  -0.00574 53  ILE A CG2 
244  C  CD1 . ILE A 38  ? 0.12029 0.13574 0.11804 -0.00789 0.00441  -0.00742 53  ILE A CD1 
245  N  N   . THR A 39  ? 0.12120 0.12634 0.10552 -0.00891 -0.00240 -0.00429 54  THR A N   
246  C  CA  . THR A 39  ? 0.12181 0.12342 0.09995 -0.00807 -0.00268 -0.00287 54  THR A CA  
247  C  C   . THR A 39  ? 0.16808 0.16206 0.13825 -0.00928 -0.00743 -0.00340 54  THR A C   
248  O  O   . THR A 39  ? 0.18558 0.17182 0.14401 -0.00755 -0.00747 -0.00319 54  THR A O   
249  C  CB  . THR A 39  ? 0.15413 0.16060 0.13954 -0.00899 -0.00301 -0.00119 54  THR A CB  
250  O  OG1 . THR A 39  ? 0.14416 0.15543 0.13482 -0.00852 0.00016  -0.00005 54  THR A OG1 
251  C  CG2 . THR A 39  ? 0.15696 0.15983 0.13638 -0.00857 -0.00385 0.00061  54  THR A CG2 
252  N  N   . ARG A 40  ? 0.14698 0.14277 0.12292 -0.01216 -0.01167 -0.00351 55  ARG A N   
253  C  CA  . ARG A 40  ? 0.15260 0.14169 0.12253 -0.01448 -0.01775 -0.00294 55  ARG A CA  
254  C  C   . ARG A 40  ? 0.19004 0.16933 0.14934 -0.01505 -0.02016 -0.00444 55  ARG A C   
255  O  O   . ARG A 40  ? 0.21859 0.18699 0.16593 -0.01595 -0.02495 -0.00449 55  ARG A O   
256  C  CB  . ARG A 40  ? 0.18091 0.17737 0.16288 -0.01736 -0.02157 -0.00084 55  ARG A CB  
257  C  CG  . ARG A 40  ? 0.29218 0.29205 0.27818 -0.01668 -0.02199 0.00084  55  ARG A CG  
258  C  CD  . ARG A 40  ? 0.32859 0.33831 0.32763 -0.01579 -0.02004 0.00191  55  ARG A CD  
259  N  NE  . ARG A 40  ? 0.36699 0.37830 0.36861 -0.01440 -0.02014 0.00322  55  ARG A NE  
260  C  CZ  . ARG A 40  ? 0.38917 0.40109 0.39135 -0.01234 -0.01653 0.00246  55  ARG A CZ  
261  N  NH1 . ARG A 40  ? 0.31536 0.32722 0.31615 -0.01157 -0.01259 0.00072  55  ARG A NH1 
262  N  NH2 . ARG A 40  ? 0.41182 0.42405 0.41618 -0.01131 -0.01757 0.00394  55  ARG A NH2 
263  N  N   . ASN A 41  ? 0.16848 0.14968 0.13038 -0.01454 -0.01757 -0.00566 56  ASN A N   
264  C  CA  . ASN A 41  ? 0.17083 0.14101 0.12125 -0.01449 -0.01966 -0.00723 56  ASN A CA  
265  C  C   . ASN A 41  ? 0.15379 0.12735 0.10620 -0.01135 -0.01357 -0.00857 56  ASN A C   
266  O  O   . ASN A 41  ? 0.15152 0.13223 0.11399 -0.01309 -0.01298 -0.00835 56  ASN A O   
267  C  CB  . ASN A 41  ? 0.21042 0.17891 0.16417 -0.01991 -0.02689 -0.00583 56  ASN A CB  
268  C  CG  . ASN A 41  ? 0.21095 0.16483 0.15061 -0.02050 -0.03066 -0.00738 56  ASN A CG  
269  O  OD1 . ASN A 41  ? 0.22468 0.17013 0.15214 -0.01571 -0.02676 -0.00988 56  ASN A OD1 
270  N  ND2 . ASN A 41  ? 0.26004 0.21063 0.20133 -0.02627 -0.03851 -0.00528 56  ASN A ND2 
271  N  N   . PRO A 42  ? 0.16004 0.12917 0.10325 -0.00633 -0.00873 -0.00936 57  PRO A N   
272  C  CA  . PRO A 42  ? 0.17480 0.14853 0.12135 -0.00317 -0.00309 -0.00968 57  PRO A CA  
273  C  C   . PRO A 42  ? 0.16703 0.13124 0.10472 -0.00209 -0.00429 -0.01141 57  PRO A C   
274  O  O   . PRO A 42  ? 0.18945 0.15607 0.12815 0.00132  0.00029  -0.01149 57  PRO A O   
275  C  CB  . PRO A 42  ? 0.17536 0.14981 0.11696 0.00205  0.00267  -0.00822 57  PRO A CB  
276  C  CG  . PRO A 42  ? 0.19870 0.16074 0.12496 0.00326  -0.00017 -0.00874 57  PRO A CG  
277  C  CD  . PRO A 42  ? 0.22687 0.18825 0.15736 -0.00290 -0.00763 -0.00906 57  PRO A CD  
278  N  N   . LEU A 43  ? 0.18753 0.14067 0.11683 -0.00527 -0.01105 -0.01232 58  LEU A N   
279  C  CA  . LEU A 43  ? 0.19275 0.13331 0.11082 -0.00459 -0.01353 -0.01393 58  LEU A CA  
280  C  C   . LEU A 43  ? 0.20697 0.15195 0.13529 -0.01030 -0.01754 -0.01313 58  LEU A C   
281  O  O   . LEU A 43  ? 0.23315 0.16629 0.15238 -0.01179 -0.02205 -0.01384 58  LEU A O   
282  C  CB  . LEU A 43  ? 0.21738 0.13874 0.11555 -0.00437 -0.01952 -0.01515 58  LEU A CB  
283  C  CG  . LEU A 43  ? 0.25685 0.17341 0.14347 0.00164  -0.01529 -0.01542 58  LEU A CG  
284  C  CD1 . LEU A 43  ? 0.31353 0.20873 0.17805 0.00160  -0.02234 -0.01685 58  LEU A CD1 
285  C  CD2 . LEU A 43  ? 0.28121 0.19936 0.16394 0.00999  -0.00607 -0.01555 58  LEU A CD2 
286  N  N   . VAL A 44  ? 0.17348 0.13418 0.11928 -0.01313 -0.01591 -0.01140 59  VAL A N   
287  C  CA  . VAL A 44  ? 0.17803 0.14494 0.13451 -0.01802 -0.01873 -0.00961 59  VAL A CA  
288  C  C   . VAL A 44  ? 0.17544 0.15117 0.13979 -0.01563 -0.01277 -0.01006 59  VAL A C   
289  O  O   . VAL A 44  ? 0.15626 0.14263 0.12965 -0.01409 -0.00844 -0.00979 59  VAL A O   
290  C  CB  . VAL A 44  ? 0.17697 0.15412 0.14589 -0.02217 -0.02144 -0.00667 59  VAL A CB  
291  C  CG1 . VAL A 44  ? 0.20556 0.19025 0.18571 -0.02645 -0.02343 -0.00358 59  VAL A CG1 
292  C  CG2 . VAL A 44  ? 0.19039 0.15891 0.15158 -0.02466 -0.02800 -0.00584 59  VAL A CG2 
293  N  N   . ALA A 45  ? 0.17923 0.14916 0.13921 -0.01557 -0.01335 -0.01062 60  ALA A N   
294  C  CA  . ALA A 45  ? 0.14438 0.12061 0.10954 -0.01293 -0.00823 -0.01107 60  ALA A CA  
295  C  C   . ALA A 45  ? 0.14069 0.13034 0.12017 -0.01535 -0.00666 -0.00933 60  ALA A C   
296  O  O   . ALA A 45  ? 0.14837 0.14493 0.13300 -0.01295 -0.00233 -0.00974 60  ALA A O   
297  C  CB  . ALA A 45  ? 0.17056 0.13687 0.12774 -0.01272 -0.01002 -0.01167 60  ALA A CB  
298  N  N   . VAL A 46  ? 0.15080 0.14384 0.13628 -0.01982 -0.01032 -0.00686 61  VAL A N   
299  C  CA  . VAL A 46  ? 0.14290 0.14786 0.14035 -0.02083 -0.00810 -0.00467 61  VAL A CA  
300  C  C   . VAL A 46  ? 0.11010 0.12217 0.11238 -0.01798 -0.00441 -0.00551 61  VAL A C   
301  O  O   . VAL A 46  ? 0.12328 0.14181 0.13094 -0.01649 -0.00113 -0.00528 61  VAL A O   
302  C  CB  . VAL A 46  ? 0.13306 0.14146 0.13689 -0.02571 -0.01254 -0.00038 61  VAL A CB  
303  C  CG1 . VAL A 46  ? 0.21183 0.23304 0.22734 -0.02494 -0.00968 0.00235  61  VAL A CG1 
304  C  CG2 . VAL A 46  ? 0.19088 0.19641 0.19418 -0.02876 -0.01471 0.00163  61  VAL A CG2 
305  N  N   . TYR A 47  ? 0.14671 0.15624 0.14570 -0.01705 -0.00517 -0.00646 62  TYR A N   
306  C  CA  . TYR A 47  ? 0.11760 0.13244 0.12044 -0.01470 -0.00226 -0.00702 62  TYR A CA  
307  C  C   . TYR A 47  ? 0.10507 0.12074 0.10720 -0.01210 0.00136  -0.00851 62  TYR A C   
308  O  O   . TYR A 47  ? 0.09562 0.11565 0.10195 -0.01106 0.00312  -0.00854 62  TYR A O   
309  C  CB  . TYR A 47  ? 0.12232 0.13378 0.12103 -0.01426 -0.00366 -0.00733 62  TYR A CB  
310  C  CG  . TYR A 47  ? 0.13864 0.14866 0.13764 -0.01711 -0.00834 -0.00553 62  TYR A CG  
311  C  CD1 . TYR A 47  ? 0.15432 0.16911 0.16048 -0.02001 -0.01078 -0.00269 62  TYR A CD1 
312  C  CD2 . TYR A 47  ? 0.14307 0.14729 0.13534 -0.01699 -0.01057 -0.00588 62  TYR A CD2 
313  C  CE1 . TYR A 47  ? 0.14635 0.16076 0.15426 -0.02331 -0.01607 0.00012  62  TYR A CE1 
314  C  CE2 . TYR A 47  ? 0.15152 0.15361 0.14355 -0.02008 -0.01601 -0.00390 62  TYR A CE2 
315  C  CZ  . TYR A 47  ? 0.17256 0.18010 0.17312 -0.02353 -0.01912 -0.00072 62  TYR A CZ  
316  O  OH  . TYR A 47  ? 0.17910 0.18550 0.18095 -0.02726 -0.02548 0.00237  62  TYR A OH  
317  N  N   . TYR A 48  ? 0.10570 0.11640 0.10191 -0.01084 0.00205  -0.00941 63  TYR A N   
318  C  CA  . TYR A 48  ? 0.12483 0.13735 0.12161 -0.00853 0.00496  -0.00968 63  TYR A CA  
319  C  C   . TYR A 48  ? 0.11350 0.12850 0.11354 -0.00913 0.00551  -0.00966 63  TYR A C   
320  O  O   . TYR A 48  ? 0.11173 0.12998 0.11474 -0.00841 0.00669  -0.00951 63  TYR A O   
321  C  CB  . TYR A 48  ? 0.12557 0.13263 0.11516 -0.00575 0.00620  -0.00987 63  TYR A CB  
322  C  CG  . TYR A 48  ? 0.12858 0.13265 0.11306 -0.00401 0.00667  -0.00957 63  TYR A CG  
323  C  CD1 . TYR A 48  ? 0.14790 0.15712 0.13572 -0.00240 0.00918  -0.00790 63  TYR A CD1 
324  C  CD2 . TYR A 48  ? 0.15499 0.15027 0.13056 -0.00430 0.00404  -0.01050 63  TYR A CD2 
325  C  CE1 . TYR A 48  ? 0.15511 0.16179 0.13774 -0.00054 0.01013  -0.00706 63  TYR A CE1 
326  C  CE2 . TYR A 48  ? 0.17135 0.16246 0.14010 -0.00228 0.00446  -0.01028 63  TYR A CE2 
327  C  CZ  . TYR A 48  ? 0.17325 0.17053 0.14562 -0.00013 0.00802  -0.00853 63  TYR A CZ  
328  O  OH  . TYR A 48  ? 0.19128 0.18437 0.15618 0.00213  0.00887  -0.00783 63  TYR A OH  
329  N  N   . THR A 49  ? 0.11346 0.12616 0.11229 -0.01074 0.00414  -0.00942 64  THR A N   
330  C  CA  . THR A 49  ? 0.11982 0.13510 0.12130 -0.01111 0.00507  -0.00896 64  THR A CA  
331  C  C   . THR A 49  ? 0.11083 0.13156 0.11723 -0.01123 0.00601  -0.00825 64  THR A C   
332  O  O   . THR A 49  ? 0.10132 0.12331 0.10797 -0.01011 0.00742  -0.00846 64  THR A O   
333  C  CB  . THR A 49  ? 0.13364 0.14526 0.13290 -0.01309 0.00334  -0.00802 64  THR A CB  
334  O  OG1 . THR A 49  ? 0.13895 0.14972 0.13907 -0.01602 0.00038  -0.00652 64  THR A OG1 
335  C  CG2 . THR A 49  ? 0.16961 0.17389 0.16186 -0.01137 0.00304  -0.00911 64  THR A CG2 
336  N  N   . ASN A 50  ? 0.08659 0.10968 0.09586 -0.01202 0.00515  -0.00728 65  ASN A N   
337  C  CA  . ASN A 50  ? 0.09145 0.11900 0.10433 -0.01049 0.00677  -0.00653 65  ASN A CA  
338  C  C   . ASN A 50  ? 0.10718 0.13287 0.11783 -0.00845 0.00748  -0.00844 65  ASN A C   
339  O  O   . ASN A 50  ? 0.09295 0.11813 0.10213 -0.00658 0.00873  -0.00883 65  ASN A O   
340  C  CB  . ASN A 50  ? 0.08722 0.11806 0.10429 -0.01122 0.00553  -0.00465 65  ASN A CB  
341  C  CG  . ASN A 50  ? 0.13289 0.16809 0.15497 -0.01351 0.00453  -0.00093 65  ASN A CG  
342  O  OD1 . ASN A 50  ? 0.11230 0.14722 0.13406 -0.01496 0.00461  0.00016  65  ASN A OD1 
343  N  ND2 . ASN A 50  ? 0.11948 0.15912 0.14695 -0.01423 0.00309  0.00180  65  ASN A ND2 
344  N  N   . ARG A 51  ? 0.07970 0.10354 0.08924 -0.00885 0.00638  -0.00918 66  ARG A N   
345  C  CA  . ARG A 51  ? 0.07332 0.09581 0.08201 -0.00806 0.00606  -0.00977 66  ARG A CA  
346  C  C   . ARG A 51  ? 0.10180 0.12299 0.10897 -0.00805 0.00599  -0.00995 66  ARG A C   
347  O  O   . ARG A 51  ? 0.10977 0.12862 0.11529 -0.00776 0.00484  -0.01023 66  ARG A O   
348  C  CB  . ARG A 51  ? 0.09331 0.11565 0.10224 -0.00859 0.00533  -0.00922 66  ARG A CB  
349  C  CG  . ARG A 51  ? 0.10368 0.12505 0.11309 -0.00875 0.00409  -0.00869 66  ARG A CG  
350  C  CD  . ARG A 51  ? 0.11330 0.13539 0.12348 -0.00925 0.00376  -0.00733 66  ARG A CD  
351  N  NE  . ARG A 51  ? 0.10241 0.12620 0.11237 -0.00887 0.00530  -0.00592 66  ARG A NE  
352  C  CZ  . ARG A 51  ? 0.12705 0.15191 0.13682 -0.00849 0.00609  -0.00395 66  ARG A CZ  
353  N  NH1 . ARG A 51  ? 0.13338 0.15774 0.14369 -0.00933 0.00484  -0.00320 66  ARG A NH1 
354  N  NH2 . ARG A 51  ? 0.12749 0.15357 0.13578 -0.00659 0.00856  -0.00243 66  ARG A NH2 
355  N  N   . ALA A 52  ? 0.11841 0.13985 0.12518 -0.00833 0.00659  -0.00968 67  ALA A N   
356  C  CA  . ALA A 52  ? 0.09947 0.12026 0.10547 -0.00820 0.00629  -0.00934 67  ALA A CA  
357  C  C   . ALA A 52  ? 0.11467 0.13354 0.11810 -0.00781 0.00617  -0.01004 67  ALA A C   
358  O  O   . ALA A 52  ? 0.11152 0.12800 0.11294 -0.00793 0.00447  -0.00997 67  ALA A O   
359  C  CB  . ALA A 52  ? 0.11347 0.13378 0.11849 -0.00777 0.00717  -0.00897 67  ALA A CB  
360  N  N   . LEU A 53  ? 0.09391 0.11368 0.09706 -0.00726 0.00779  -0.01010 68  LEU A N   
361  C  CA  . LEU A 53  ? 0.09404 0.11223 0.09370 -0.00559 0.00897  -0.01019 68  LEU A CA  
362  C  C   . LEU A 53  ? 0.12366 0.13773 0.11935 -0.00373 0.00812  -0.01130 68  LEU A C   
363  O  O   . LEU A 53  ? 0.11791 0.12651 0.10707 -0.00234 0.00740  -0.01206 68  LEU A O   
364  C  CB  . LEU A 53  ? 0.11639 0.13872 0.11865 -0.00517 0.01143  -0.00843 68  LEU A CB  
365  C  CG  . LEU A 53  ? 0.12580 0.14818 0.12477 -0.00227 0.01430  -0.00736 68  LEU A CG  
366  C  CD1 . LEU A 53  ? 0.14891 0.16694 0.14212 -0.00214 0.01389  -0.00799 68  LEU A CD1 
367  C  CD2 . LEU A 53  ? 0.11787 0.14727 0.12281 -0.00281 0.01654  -0.00376 68  LEU A CD2 
368  N  N   . CYS A 54  ? 0.10279 0.11769 0.10081 -0.00366 0.00763  -0.01144 69  CYS A N   
369  C  CA  . CYS A 54  ? 0.11669 0.12564 0.10989 -0.00206 0.00597  -0.01250 69  CYS A CA  
370  C  C   . CYS A 54  ? 0.11917 0.12284 0.10931 -0.00428 0.00183  -0.01276 69  CYS A C   
371  O  O   . CYS A 54  ? 0.12406 0.11935 0.10619 -0.00318 -0.00049 -0.01378 69  CYS A O   
372  C  CB  . CYS A 54  ? 0.10079 0.11168 0.09773 -0.00221 0.00561  -0.01218 69  CYS A CB  
373  S  SG  . CYS A 54  ? 0.14116 0.15819 0.14247 0.00031  0.00909  -0.01076 69  CYS A SG  
374  N  N   . TYR A 55  ? 0.10380 0.11190 0.09985 -0.00721 0.00059  -0.01132 70  TYR A N   
375  C  CA  . TYR A 55  ? 0.11891 0.12483 0.11512 -0.00979 -0.00352 -0.00984 70  TYR A CA  
376  C  C   . TYR A 55  ? 0.12290 0.12480 0.11415 -0.00971 -0.00501 -0.01016 70  TYR A C   
377  O  O   . TYR A 55  ? 0.12472 0.12029 0.11176 -0.01140 -0.00986 -0.00958 70  TYR A O   
378  C  CB  . TYR A 55  ? 0.11775 0.13121 0.12202 -0.01150 -0.00293 -0.00717 70  TYR A CB  
379  C  CG  . TYR A 55  ? 0.13309 0.14900 0.14080 -0.01203 -0.00258 -0.00615 70  TYR A CG  
380  C  CD1 . TYR A 55  ? 0.14339 0.15442 0.14884 -0.01302 -0.00560 -0.00613 70  TYR A CD1 
381  C  CD2 . TYR A 55  ? 0.12712 0.14857 0.13866 -0.01127 0.00048  -0.00517 70  TYR A CD2 
382  C  CE1 . TYR A 55  ? 0.17390 0.18703 0.18236 -0.01365 -0.00541 -0.00483 70  TYR A CE1 
383  C  CE2 . TYR A 55  ? 0.11944 0.14247 0.13284 -0.01156 0.00084  -0.00404 70  TYR A CE2 
384  C  CZ  . TYR A 55  ? 0.15758 0.17723 0.17020 -0.01292 -0.00199 -0.00371 70  TYR A CZ  
385  O  OH  . TYR A 55  ? 0.14546 0.16655 0.15980 -0.01333 -0.00174 -0.00226 70  TYR A OH  
386  N  N   . LEU A 56  ? 0.10845 0.11313 0.09962 -0.00823 -0.00164 -0.01072 71  LEU A N   
387  C  CA  . LEU A 56  ? 0.14023 0.14050 0.12555 -0.00784 -0.00281 -0.01097 71  LEU A CA  
388  C  C   . LEU A 56  ? 0.16373 0.15404 0.13786 -0.00549 -0.00394 -0.01289 71  LEU A C   
389  O  O   . LEU A 56  ? 0.17554 0.15773 0.14214 -0.00622 -0.00822 -0.01306 71  LEU A O   
390  C  CB  . LEU A 56  ? 0.15017 0.15469 0.13700 -0.00671 0.00115  -0.01085 71  LEU A CB  
391  C  CG  . LEU A 56  ? 0.17127 0.18135 0.16477 -0.00813 0.00139  -0.00921 71  LEU A CG  
392  C  CD1 . LEU A 56  ? 0.16790 0.17996 0.16163 -0.00740 0.00455  -0.00920 71  LEU A CD1 
393  C  CD2 . LEU A 56  ? 0.22239 0.23095 0.21562 -0.00946 -0.00234 -0.00758 71  LEU A CD2 
394  N  N   . LYS A 57  ? 0.15597 0.14598 0.12797 -0.00220 -0.00031 -0.01408 72  LYS A N   
395  C  CA  . LYS A 57  ? 0.16876 0.14827 0.12842 0.00183  -0.00035 -0.01583 72  LYS A CA  
396  C  C   . LYS A 57  ? 0.17349 0.14235 0.12672 0.00010  -0.00687 -0.01668 72  LYS A C   
397  O  O   . LYS A 57  ? 0.19616 0.15165 0.13545 0.00233  -0.00969 -0.01830 72  LYS A O   
398  C  CB  . LYS A 57  ? 0.20186 0.18510 0.16272 0.00629  0.00516  -0.01585 72  LYS A CB  
399  C  CG  . LYS A 57  ? 0.22053 0.21363 0.18743 0.00763  0.01082  -0.01388 72  LYS A CG  
400  C  CD  . LYS A 57  ? 0.30681 0.29521 0.26388 0.01185  0.01382  -0.01365 72  LYS A CD  
401  C  CE  . LYS A 57  ? 0.37907 0.37841 0.34361 0.01261  0.01931  -0.01035 72  LYS A CE  
402  N  NZ  . LYS A 57  ? 0.44921 0.44478 0.40387 0.01773  0.02346  -0.00923 72  LYS A NZ  
403  N  N   . MET A 58  ? 0.16342 0.13699 0.12560 -0.00382 -0.00956 -0.01528 73  MET A N   
404  C  CA  . MET A 58  ? 0.17866 0.14374 0.13736 -0.00687 -0.01644 -0.01475 73  MET A CA  
405  C  C   . MET A 58  ? 0.19380 0.15794 0.15459 -0.01212 -0.02286 -0.01214 73  MET A C   
406  O  O   . MET A 58  ? 0.19853 0.15714 0.15880 -0.01617 -0.02973 -0.01022 73  MET A O   
407  C  CB  . MET A 58  ? 0.15663 0.12849 0.12483 -0.00860 -0.01588 -0.01334 73  MET A CB  
408  C  CG  . MET A 58  ? 0.19401 0.16631 0.16071 -0.00385 -0.01099 -0.01519 73  MET A CG  
409  S  SD  . MET A 58  ? 0.18669 0.17124 0.16670 -0.00571 -0.00844 -0.01330 73  MET A SD  
410  C  CE  . MET A 58  ? 0.25527 0.23536 0.23673 -0.01094 -0.01548 -0.01073 73  MET A CE  
411  N  N   . GLN A 59  ? 0.17514 0.14478 0.13891 -0.01238 -0.02124 -0.01134 74  GLN A N   
412  C  CA  . GLN A 59  ? 0.19672 0.16751 0.16422 -0.01685 -0.02692 -0.00806 74  GLN A CA  
413  C  C   . GLN A 59  ? 0.21081 0.19284 0.19304 -0.02091 -0.02837 -0.00344 74  GLN A C   
414  O  O   . GLN A 59  ? 0.21105 0.19362 0.19759 -0.02542 -0.03479 0.00081  74  GLN A O   
415  C  CB  . GLN A 59  ? 0.27388 0.22860 0.22807 -0.01882 -0.03546 -0.00842 74  GLN A CB  
416  C  CG  . GLN A 59  ? 0.34593 0.28663 0.28213 -0.01330 -0.03355 -0.01309 74  GLN A CG  
417  C  CD  . GLN A 59  ? 0.40974 0.34789 0.33909 -0.01144 -0.03243 -0.01382 74  GLN A CD  
418  O  OE1 . GLN A 59  ? 0.40308 0.35340 0.34271 -0.01196 -0.02865 -0.01217 74  GLN A OE1 
419  N  NE2 . GLN A 59  ? 0.44571 0.36645 0.35596 -0.00886 -0.03584 -0.01630 74  GLN A NE2 
420  N  N   . GLN A 60  ? 0.17063 0.16194 0.16069 -0.01924 -0.02250 -0.00354 75  GLN A N   
421  C  CA  . GLN A 60  ? 0.16118 0.16310 0.16370 -0.02167 -0.02227 0.00096  75  GLN A CA  
422  C  C   . GLN A 60  ? 0.16548 0.17807 0.17543 -0.01949 -0.01673 0.00212  75  GLN A C   
423  O  O   . GLN A 60  ? 0.14449 0.16251 0.15762 -0.01712 -0.01137 0.00127  75  GLN A O   
424  C  CB  . GLN A 60  ? 0.16801 0.17021 0.17145 -0.02110 -0.02035 0.00012  75  GLN A CB  
425  C  CG  . GLN A 60  ? 0.18295 0.17342 0.17886 -0.02325 -0.02656 -0.00040 75  GLN A CG  
426  C  CD  . GLN A 60  ? 0.28020 0.27187 0.27861 -0.02323 -0.02531 -0.00009 75  GLN A CD  
427  O  OE1 . GLN A 60  ? 0.33401 0.33615 0.34090 -0.02257 -0.02070 0.00161  75  GLN A OE1 
428  N  NE2 . GLN A 60  ? 0.30373 0.28322 0.29326 -0.02357 -0.02963 -0.00175 75  GLN A NE2 
429  N  N   . HIS A 61  ? 0.19222 0.20620 0.20361 -0.02020 -0.01872 0.00411  76  HIS A N   
430  C  CA  . HIS A 61  ? 0.18381 0.20454 0.19904 -0.01730 -0.01380 0.00441  76  HIS A CA  
431  C  C   . HIS A 61  ? 0.15588 0.18716 0.18109 -0.01607 -0.01028 0.00843  76  HIS A C   
432  O  O   . HIS A 61  ? 0.13315 0.16709 0.15825 -0.01250 -0.00495 0.00705  76  HIS A O   
433  C  CB  . HIS A 61  ? 0.21534 0.23472 0.22969 -0.01818 -0.01720 0.00607  76  HIS A CB  
434  C  CG  . HIS A 61  ? 0.24866 0.25644 0.25096 -0.01864 -0.02035 0.00239  76  HIS A CG  
435  N  ND1 . HIS A 61  ? 0.26231 0.26102 0.25843 -0.02174 -0.02729 0.00266  76  HIS A ND1 
436  C  CD2 . HIS A 61  ? 0.31090 0.31378 0.30501 -0.01600 -0.01740 -0.00129 76  HIS A CD2 
437  C  CE1 . HIS A 61  ? 0.29622 0.28410 0.27934 -0.02008 -0.02795 -0.00117 76  HIS A CE1 
438  N  NE2 . HIS A 61  ? 0.29440 0.28583 0.27705 -0.01662 -0.02162 -0.00323 76  HIS A NE2 
439  N  N   . GLU A 62  ? 0.15227 0.18888 0.18529 -0.01880 -0.01329 0.01380  77  GLU A N   
440  C  CA  . GLU A 62  ? 0.14470 0.19189 0.18661 -0.01661 -0.00884 0.01841  77  GLU A CA  
441  C  C   . GLU A 62  ? 0.16551 0.21116 0.20332 -0.01401 -0.00383 0.01480  77  GLU A C   
442  O  O   . GLU A 62  ? 0.15232 0.20168 0.19047 -0.00974 0.00174  0.01504  77  GLU A O   
443  C  CB  . GLU A 62  ? 0.21081 0.26494 0.26292 -0.02074 -0.01329 0.02609  77  GLU A CB  
444  N  N   . GLN A 63  ? 0.15116 0.19023 0.18398 -0.01619 -0.00606 0.01153  78  GLN A N   
445  C  CA  . GLN A 63  ? 0.13538 0.17281 0.16446 -0.01408 -0.00218 0.00829  78  GLN A CA  
446  C  C   . GLN A 63  ? 0.14519 0.17892 0.16800 -0.01105 0.00123  0.00340  78  GLN A C   
447  O  O   . GLN A 63  ? 0.12372 0.15782 0.14458 -0.00864 0.00484  0.00217  78  GLN A O   
448  C  CB  . GLN A 63  ? 0.17627 0.20745 0.20177 -0.01664 -0.00561 0.00638  78  GLN A CB  
449  C  CG  . GLN A 63  ? 0.20658 0.24060 0.23794 -0.02015 -0.00912 0.01161  78  GLN A CG  
450  C  CD  . GLN A 63  ? 0.28123 0.31618 0.31716 -0.02414 -0.01505 0.01623  78  GLN A CD  
451  O  OE1 . GLN A 63  ? 0.33491 0.36251 0.36518 -0.02529 -0.01899 0.01374  78  GLN A OE1 
452  N  NE2 . GLN A 63  ? 0.37034 0.41457 0.41659 -0.02630 -0.01589 0.02370  78  GLN A NE2 
453  N  N   . ALA A 64  ? 0.12247 0.15180 0.14136 -0.01146 -0.00040 0.00096  79  ALA A N   
454  C  CA  . ALA A 64  ? 0.13666 0.16332 0.15088 -0.00937 0.00236  -0.00240 79  ALA A CA  
455  C  C   . ALA A 64  ? 0.13016 0.15969 0.14561 -0.00670 0.00531  -0.00099 79  ALA A C   
456  O  O   . ALA A 64  ? 0.11397 0.14106 0.12563 -0.00496 0.00768  -0.00296 79  ALA A O   
457  C  CB  . ALA A 64  ? 0.13291 0.15488 0.14269 -0.01010 0.00038  -0.00421 79  ALA A CB  
458  N  N   . LEU A 65  ? 0.12043 0.15444 0.14072 -0.00617 0.00476  0.00281  80  LEU A N   
459  C  CA  . LEU A 65  ? 0.12185 0.15787 0.14240 -0.00221 0.00805  0.00443  80  LEU A CA  
460  C  C   . LEU A 65  ? 0.12440 0.16133 0.14348 0.00100  0.01194  0.00502  80  LEU A C   
461  O  O   . LEU A 65  ? 0.12230 0.15446 0.13497 0.00444  0.01453  0.00321  80  LEU A O   
462  C  CB  . LEU A 65  ? 0.16723 0.20984 0.19516 -0.00185 0.00681  0.00967  80  LEU A CB  
463  C  CG  . LEU A 65  ? 0.20740 0.25213 0.23561 0.00351  0.01054  0.01192  80  LEU A CG  
464  C  CD1 . LEU A 65  ? 0.24975 0.29604 0.28117 0.00285  0.00770  0.01410  80  LEU A CD1 
465  C  CD2 . LEU A 65  ? 0.26109 0.31423 0.29553 0.00712  0.01424  0.01748  80  LEU A CD2 
466  N  N   . ALA A 66  ? 0.13191 0.17340 0.15541 -0.00017 0.01190  0.00760  81  ALA A N   
467  C  CA  . ALA A 66  ? 0.14772 0.18958 0.16859 0.00306  0.01572  0.00842  81  ALA A CA  
468  C  C   . ALA A 66  ? 0.12916 0.16224 0.14067 0.00318  0.01583  0.00309  81  ALA A C   
469  O  O   . ALA A 66  ? 0.12037 0.14903 0.12480 0.00707  0.01863  0.00238  81  ALA A O   
470  C  CB  . ALA A 66  ? 0.13631 0.18430 0.16372 0.00070  0.01494  0.01233  81  ALA A CB  
471  N  N   . ASP A 67  ? 0.13612 0.16614 0.14697 -0.00077 0.01263  -0.00019 82  ASP A N   
472  C  CA  . ASP A 67  ? 0.12909 0.15277 0.13355 -0.00131 0.01209  -0.00385 82  ASP A CA  
473  C  C   . ASP A 67  ? 0.14009 0.15799 0.13880 0.00002  0.01224  -0.00568 82  ASP A C   
474  O  O   . ASP A 67  ? 0.11913 0.13049 0.11085 0.00073  0.01195  -0.00732 82  ASP A O   
475  C  CB  . ASP A 67  ? 0.08951 0.11308 0.09599 -0.00483 0.00946  -0.00568 82  ASP A CB  
476  C  CG  . ASP A 67  ? 0.13570 0.16067 0.14384 -0.00584 0.00885  -0.00507 82  ASP A CG  
477  O  OD1 . ASP A 67  ? 0.12876 0.15403 0.13531 -0.00422 0.01047  -0.00368 82  ASP A OD1 
478  O  OD2 . ASP A 67  ? 0.11676 0.14160 0.12658 -0.00771 0.00694  -0.00591 82  ASP A OD2 
479  N  N   . CYS A 68  ? 0.12885 0.14788 0.12961 0.00000  0.01191  -0.00520 83  CYS A N   
480  C  CA  . CYS A 68  ? 0.13693 0.14981 0.13195 0.00135  0.01188  -0.00641 83  CYS A CA  
481  C  C   . CYS A 68  ? 0.12566 0.13381 0.11398 0.00642  0.01439  -0.00576 83  CYS A C   
482  O  O   . CYS A 68  ? 0.13985 0.13842 0.11912 0.00734  0.01344  -0.00769 83  CYS A O   
483  C  CB  . CYS A 68  ? 0.11260 0.12768 0.11081 0.00095  0.01123  -0.00547 83  CYS A CB  
484  S  SG  . CYS A 68  ? 0.13171 0.14824 0.13262 -0.00347 0.00878  -0.00674 83  CYS A SG  
485  N  N   . ARG A 69  ? 0.12358 0.13773 0.11559 0.00996  0.01748  -0.00253 84  ARG A N   
486  C  CA  . ARG A 69  ? 0.13585 0.14570 0.12038 0.01651  0.02125  -0.00134 84  ARG A CA  
487  C  C   . ARG A 69  ? 0.16639 0.16838 0.14141 0.01707  0.02112  -0.00356 84  ARG A C   
488  O  O   . ARG A 69  ? 0.16065 0.15104 0.12285 0.02103  0.02163  -0.00527 84  ARG A O   
489  C  CB  . ARG A 69  ? 0.17246 0.19331 0.16531 0.02025  0.02521  0.00422  84  ARG A CB  
490  C  CG  . ARG A 69  ? 0.16180 0.18982 0.16339 0.02037  0.02485  0.00738  84  ARG A CG  
491  C  CD  . ARG A 69  ? 0.16961 0.19068 0.16378 0.02602  0.02670  0.00690  84  ARG A CD  
492  N  NE  . ARG A 69  ? 0.18398 0.21274 0.18732 0.02617  0.02608  0.01055  84  ARG A NE  
493  C  CZ  . ARG A 69  ? 0.19747 0.22053 0.19704 0.02719  0.02474  0.00913  84  ARG A CZ  
494  N  NH1 . ARG A 69  ? 0.18423 0.19370 0.17122 0.02802  0.02382  0.00449  84  ARG A NH1 
495  N  NH2 . ARG A 69  ? 0.21451 0.24517 0.22305 0.02681  0.02353  0.01287  84  ARG A NH2 
496  N  N   . ARG A 70  ? 0.13628 0.14280 0.11603 0.01321  0.01981  -0.00359 85  ARG A N   
497  C  CA  . ARG A 70  ? 0.15837 0.15729 0.12928 0.01310  0.01876  -0.00554 85  ARG A CA  
498  C  C   . ARG A 70  ? 0.14903 0.13692 0.11191 0.01017  0.01415  -0.00912 85  ARG A C   
499  O  O   . ARG A 70  ? 0.19805 0.17406 0.14805 0.01219  0.01291  -0.01069 85  ARG A O   
500  C  CB  . ARG A 70  ? 0.15126 0.15732 0.12973 0.00918  0.01767  -0.00469 85  ARG A CB  
501  C  CG  . ARG A 70  ? 0.18714 0.20235 0.17190 0.01164  0.02151  -0.00022 85  ARG A CG  
502  C  CD  . ARG A 70  ? 0.23489 0.25711 0.22886 0.00675  0.01929  0.00088  85  ARG A CD  
503  N  NE  . ARG A 70  ? 0.28031 0.31231 0.28285 0.00756  0.02167  0.00629  85  ARG A NE  
504  C  CZ  . ARG A 70  ? 0.28834 0.32687 0.30078 0.00335  0.01899  0.00831  85  ARG A CZ  
505  N  NH1 . ARG A 70  ? 0.11881 0.15465 0.13245 -0.00076 0.01487  0.00490  85  ARG A NH1 
506  N  NH2 . ARG A 70  ? 0.32415 0.37159 0.34488 0.00343  0.02032  0.01441  85  ARG A NH2 
507  N  N   . ALA A 71  ? 0.15589 0.14696 0.12557 0.00538  0.01127  -0.00990 86  ALA A N   
508  C  CA  . ALA A 71  ? 0.13682 0.11966 0.10147 0.00183  0.00674  -0.01169 86  ALA A CA  
509  C  C   . ALA A 71  ? 0.16240 0.13310 0.11538 0.00517  0.00624  -0.01263 86  ALA A C   
510  O  O   . ALA A 71  ? 0.18283 0.14116 0.12517 0.00394  0.00214  -0.01399 86  ALA A O   
511  C  CB  . ALA A 71  ? 0.12833 0.11839 0.10285 -0.00271 0.00526  -0.01125 86  ALA A CB  
512  N  N   . LEU A 72  ? 0.16981 0.14300 0.12419 0.00930  0.00969  -0.01163 87  LEU A N   
513  C  CA  . LEU A 72  ? 0.17090 0.13186 0.11383 0.01329  0.00939  -0.01245 87  LEU A CA  
514  C  C   . LEU A 72  ? 0.19551 0.14378 0.12271 0.01952  0.01079  -0.01344 87  LEU A C   
515  O  O   . LEU A 72  ? 0.22464 0.15664 0.13725 0.02155  0.00809  -0.01522 87  LEU A O   
516  C  CB  . LEU A 72  ? 0.17300 0.14089 0.12212 0.01698  0.01305  -0.01045 87  LEU A CB  
517  C  CG  . LEU A 72  ? 0.17256 0.14760 0.13185 0.01156  0.01084  -0.00998 87  LEU A CG  
518  C  CD1 . LEU A 72  ? 0.17908 0.16309 0.14630 0.01451  0.01385  -0.00740 87  LEU A CD1 
519  C  CD2 . LEU A 72  ? 0.20177 0.16534 0.15359 0.00852  0.00635  -0.01138 87  LEU A CD2 
520  N  N   A GLU A 73  ? 0.20622 0.16048 0.13485 0.02293  0.01494  -0.01207 88  GLU A N   
521  N  N   B GLU A 73  ? 0.20790 0.16204 0.13645 0.02281  0.01483  -0.01212 88  GLU A N   
522  C  CA  A GLU A 73  ? 0.21748 0.15914 0.12951 0.02920  0.01666  -0.01289 88  GLU A CA  
523  C  CA  B GLU A 73  ? 0.21689 0.15833 0.12873 0.02928  0.01665  -0.01291 88  GLU A CA  
524  C  C   A GLU A 73  ? 0.22950 0.15650 0.12965 0.02445  0.00953  -0.01592 88  GLU A C   
525  C  C   B GLU A 73  ? 0.23153 0.15889 0.13172 0.02464  0.00978  -0.01584 88  GLU A C   
526  O  O   A GLU A 73  ? 0.26439 0.17272 0.14494 0.02862  0.00776  -0.01788 88  GLU A O   
527  O  O   B GLU A 73  ? 0.26572 0.17517 0.14641 0.02916  0.00853  -0.01766 88  GLU A O   
528  C  CB  A GLU A 73  ? 0.22255 0.17551 0.14036 0.03264  0.02237  -0.00990 88  GLU A CB  
529  C  CB  B GLU A 73  ? 0.22313 0.17606 0.14067 0.03351  0.02294  -0.00969 88  GLU A CB  
530  C  CG  A GLU A 73  ? 0.21666 0.18163 0.14296 0.03901  0.02947  -0.00547 88  GLU A CG  
531  C  CG  B GLU A 73  ? 0.24246 0.18381 0.14235 0.04257  0.02715  -0.00946 88  GLU A CG  
532  C  CD  A GLU A 73  ? 0.23937 0.21889 0.17616 0.03982  0.03393  -0.00110 88  GLU A CD  
533  C  CD  B GLU A 73  ? 0.25301 0.20856 0.16098 0.04721  0.03450  -0.00455 88  GLU A CD  
534  O  OE1 A GLU A 73  ? 0.25814 0.24008 0.19812 0.03438  0.03119  -0.00196 88  GLU A OE1 
535  O  OE1 B GLU A 73  ? 0.24865 0.21948 0.17133 0.04874  0.03868  -0.00024 88  GLU A OE1 
536  O  OE2 A GLU A 73  ? 0.24523 0.23427 0.18780 0.04587  0.04004  0.00392  88  GLU A OE2 
537  O  OE2 B GLU A 73  ? 0.30633 0.25779 0.20614 0.04892  0.03562  -0.00440 88  GLU A OE2 
538  N  N   . LEU A 74  ? 0.22070 0.15528 0.13188 0.01601  0.00508  -0.01594 89  LEU A N   
539  C  CA  . LEU A 74  ? 0.22770 0.15142 0.13116 0.01049  -0.00240 -0.01741 89  LEU A CA  
540  C  C   . LEU A 74  ? 0.23900 0.15343 0.13932 0.00531  -0.00913 -0.01801 89  LEU A C   
541  O  O   . LEU A 74  ? 0.29658 0.19502 0.18380 0.00256  -0.01615 -0.01904 89  LEU A O   
542  C  CB  . LEU A 74  ? 0.20873 0.14596 0.12646 0.00452  -0.00376 -0.01610 89  LEU A CB  
543  C  CG  . LEU A 74  ? 0.22510 0.16824 0.14375 0.00779  0.00049  -0.01528 89  LEU A CG  
544  C  CD1 . LEU A 74  ? 0.23992 0.19801 0.17511 0.00245  -0.00011 -0.01384 89  LEU A CD1 
545  C  CD2 . LEU A 74  ? 0.25937 0.18642 0.16001 0.00947  -0.00286 -0.01665 89  LEU A CD2 
546  N  N   . ASP A 75  ? 0.24710 0.17064 0.15879 0.00347  -0.00776 -0.01693 90  ASP A N   
547  C  CA  . ASP A 75  ? 0.23279 0.15032 0.14430 -0.00224 -0.01376 -0.01639 90  ASP A CA  
548  C  C   . ASP A 75  ? 0.20820 0.12813 0.12213 0.00134  -0.00988 -0.01618 90  ASP A C   
549  O  O   . ASP A 75  ? 0.19361 0.12831 0.12225 -0.00078 -0.00726 -0.01462 90  ASP A O   
550  C  CB  . ASP A 75  ? 0.22265 0.15300 0.14983 -0.01050 -0.01694 -0.01391 90  ASP A CB  
551  C  CG  . ASP A 75  ? 0.23472 0.16230 0.16459 -0.01655 -0.02217 -0.01178 90  ASP A CG  
552  O  OD1 . ASP A 75  ? 0.25065 0.16281 0.16792 -0.01565 -0.02545 -0.01265 90  ASP A OD1 
553  O  OD2 . ASP A 75  ? 0.25550 0.19620 0.19979 -0.02185 -0.02277 -0.00881 90  ASP A OD2 
554  N  N   . GLY A 76  ? 0.24509 0.14926 0.14320 0.00727  -0.00972 -0.01771 91  GLY A N   
555  C  CA  . GLY A 76  ? 0.21513 0.12036 0.11452 0.01139  -0.00635 -0.01722 91  GLY A CA  
556  C  C   . GLY A 76  ? 0.23038 0.13693 0.13643 0.00455  -0.01075 -0.01582 91  GLY A C   
557  O  O   . GLY A 76  ? 0.20532 0.11554 0.11520 0.00695  -0.00805 -0.01500 91  GLY A O   
558  N  N   . GLN A 77  ? 0.20475 0.10897 0.11270 -0.00385 -0.01746 -0.01476 92  GLN A N   
559  C  CA  . GLN A 77  ? 0.21725 0.12326 0.13178 -0.01065 -0.02157 -0.01218 92  GLN A CA  
560  C  C   . GLN A 77  ? 0.19432 0.12114 0.12817 -0.01547 -0.01913 -0.00952 92  GLN A C   
561  O  O   . GLN A 77  ? 0.21090 0.14150 0.15155 -0.02130 -0.02192 -0.00640 92  GLN A O   
562  C  CB  . GLN A 77  ? 0.22799 0.11786 0.13265 -0.01723 -0.03126 -0.01110 92  GLN A CB  
563  C  CG  . GLN A 77  ? 0.27986 0.14414 0.16106 -0.01247 -0.03512 -0.01411 92  GLN A CG  
564  C  CD  . GLN A 77  ? 0.29948 0.15623 0.17368 -0.00644 -0.03228 -0.01510 92  GLN A CD  
565  O  OE1 . GLN A 77  ? 0.31877 0.17492 0.19679 -0.01095 -0.03533 -0.01278 92  GLN A OE1 
566  N  NE2 . GLN A 77  ? 0.27100 0.12237 0.13514 0.00414  -0.02620 -0.01789 92  GLN A NE2 
567  N  N   . SER A 78  ? 0.17867 0.11828 0.12061 -0.01275 -0.01387 -0.01032 93  SER A N   
568  C  CA  . SER A 78  ? 0.15492 0.11132 0.11217 -0.01645 -0.01191 -0.00821 93  SER A CA  
569  C  C   . SER A 78  ? 0.16505 0.12952 0.12949 -0.01620 -0.00878 -0.00692 93  SER A C   
570  O  O   . SER A 78  ? 0.15116 0.11831 0.11574 -0.01137 -0.00472 -0.00821 93  SER A O   
571  C  CB  . SER A 78  ? 0.16144 0.12656 0.12329 -0.01342 -0.00783 -0.00957 93  SER A CB  
572  O  OG  . SER A 78  ? 0.15429 0.13353 0.12876 -0.01558 -0.00553 -0.00799 93  SER A OG  
573  N  N   . VAL A 79  ? 0.13877 0.10779 0.10958 -0.02145 -0.01076 -0.00367 94  VAL A N   
574  C  CA  . VAL A 79  ? 0.14327 0.11974 0.11992 -0.02134 -0.00777 -0.00209 94  VAL A CA  
575  C  C   . VAL A 79  ? 0.12326 0.11110 0.10665 -0.01820 -0.00267 -0.00328 94  VAL A C   
576  O  O   . VAL A 79  ? 0.14936 0.13889 0.13254 -0.01504 -0.00009 -0.00425 94  VAL A O   
577  C  CB  . VAL A 79  ? 0.13990 0.12048 0.12258 -0.02732 -0.01015 0.00273  94  VAL A CB  
578  C  CG1 . VAL A 79  ? 0.15228 0.14152 0.14033 -0.02649 -0.00603 0.00457  94  VAL A CG1 
579  C  CG2 . VAL A 79  ? 0.16060 0.12803 0.13577 -0.03112 -0.01634 0.00437  94  VAL A CG2 
580  N  N   . LYS A 80  ? 0.13291 0.12779 0.12193 -0.01921 -0.00191 -0.00292 95  LYS A N   
581  C  CA  . LYS A 80  ? 0.11211 0.11558 0.10608 -0.01663 0.00197  -0.00391 95  LYS A CA  
582  C  C   . LYS A 80  ? 0.11504 0.11688 0.10624 -0.01268 0.00345  -0.00665 95  LYS A C   
583  O  O   . LYS A 80  ? 0.11813 0.12412 0.11152 -0.01080 0.00546  -0.00708 95  LYS A O   
584  C  CB  . LYS A 80  ? 0.14266 0.15276 0.14249 -0.01802 0.00227  -0.00272 95  LYS A CB  
585  C  CG  . LYS A 80  ? 0.18906 0.20573 0.19476 -0.02038 0.00301  0.00141  95  LYS A CG  
586  C  CD  . LYS A 80  ? 0.19143 0.21602 0.20390 -0.02052 0.00408  0.00341  95  LYS A CD  
587  C  CE  . LYS A 80  ? 0.23343 0.26576 0.25249 -0.02219 0.00552  0.00896  95  LYS A CE  
588  N  NZ  . LYS A 80  ? 0.19724 0.23861 0.22349 -0.02074 0.00772  0.01158  95  LYS A NZ  
589  N  N   . ALA A 81  ? 0.12792 0.12351 0.11392 -0.01128 0.00233  -0.00792 96  ALA A N   
590  C  CA  . ALA A 81  ? 0.11843 0.11441 0.10308 -0.00695 0.00467  -0.00905 96  ALA A CA  
591  C  C   . ALA A 81  ? 0.12860 0.12414 0.11266 -0.00457 0.00576  -0.00845 96  ALA A C   
592  O  O   . ALA A 81  ? 0.11035 0.11171 0.09870 -0.00275 0.00743  -0.00780 96  ALA A O   
593  C  CB  . ALA A 81  ? 0.13828 0.12657 0.11532 -0.00458 0.00416  -0.01011 96  ALA A CB  
594  N  N   . HIS A 82  ? 0.11770 0.10619 0.09676 -0.00506 0.00410  -0.00814 97  HIS A N   
595  C  CA  . HIS A 82  ? 0.11351 0.10144 0.09209 -0.00278 0.00483  -0.00728 97  HIS A CA  
596  C  C   . HIS A 82  ? 0.11605 0.11122 0.10052 -0.00493 0.00518  -0.00626 97  HIS A C   
597  O  O   . HIS A 82  ? 0.10796 0.10621 0.09459 -0.00299 0.00581  -0.00542 97  HIS A O   
598  C  CB  . HIS A 82  ? 0.13683 0.11400 0.10768 -0.00305 0.00245  -0.00711 97  HIS A CB  
599  C  CG  . HIS A 82  ? 0.13993 0.10636 0.10107 0.00121  0.00219  -0.00836 97  HIS A CG  
600  N  ND1 . HIS A 82  ? 0.14338 0.10150 0.09767 -0.00031 -0.00039 -0.00961 97  HIS A ND1 
601  C  CD2 . HIS A 82  ? 0.15968 0.12147 0.11564 0.00760  0.00423  -0.00828 97  HIS A CD2 
602  C  CE1 . HIS A 82  ? 0.16309 0.11007 0.10629 0.00522  0.00007  -0.01082 97  HIS A CE1 
603  N  NE2 . HIS A 82  ? 0.15723 0.10679 0.10160 0.01058  0.00342  -0.00989 97  HIS A NE2 
604  N  N   . PHE A 83  ? 0.12341 0.12089 0.10988 -0.00860 0.00464  -0.00580 98  PHE A N   
605  C  CA  . PHE A 83  ? 0.12473 0.12690 0.11368 -0.00947 0.00551  -0.00492 98  PHE A CA  
606  C  C   . PHE A 83  ? 0.13476 0.14176 0.12664 -0.00807 0.00631  -0.00583 98  PHE A C   
607  O  O   . PHE A 83  ? 0.14423 0.15195 0.13586 -0.00730 0.00577  -0.00541 98  PHE A O   
608  C  CB  . PHE A 83  ? 0.10780 0.11241 0.09841 -0.01244 0.00590  -0.00333 98  PHE A CB  
609  C  CG  . PHE A 83  ? 0.12407 0.13203 0.11460 -0.01205 0.00771  -0.00228 98  PHE A CG  
610  C  CD1 . PHE A 83  ? 0.12948 0.13528 0.11716 -0.01259 0.00766  -0.00045 98  PHE A CD1 
611  C  CD2 . PHE A 83  ? 0.15637 0.16807 0.14794 -0.01069 0.00936  -0.00313 98  PHE A CD2 
612  C  CE1 . PHE A 83  ? 0.14370 0.15109 0.12894 -0.01152 0.00955  0.00049  98  PHE A CE1 
613  C  CE2 . PHE A 83  ? 0.15044 0.16247 0.13867 -0.00928 0.01104  -0.00250 98  PHE A CE2 
614  C  CZ  . PHE A 83  ? 0.13543 0.14541 0.12018 -0.00956 0.01134  -0.00067 98  PHE A CZ  
615  N  N   . PHE A 84  ? 0.11571 0.12516 0.10992 -0.00821 0.00680  -0.00675 99  PHE A N   
616  C  CA  . PHE A 84  ? 0.12973 0.14247 0.12627 -0.00751 0.00676  -0.00724 99  PHE A CA  
617  C  C   . PHE A 84  ? 0.11930 0.13315 0.11770 -0.00585 0.00606  -0.00622 99  PHE A C   
618  O  O   . PHE A 84  ? 0.11942 0.13509 0.11954 -0.00620 0.00449  -0.00540 99  PHE A O   
619  C  CB  . PHE A 84  ? 0.12124 0.13598 0.11984 -0.00796 0.00730  -0.00806 99  PHE A CB  
620  C  CG  . PHE A 84  ? 0.13122 0.14717 0.13016 -0.00914 0.00814  -0.00785 99  PHE A CG  
621  C  CD1 . PHE A 84  ? 0.16023 0.17644 0.15748 -0.00900 0.00916  -0.00701 99  PHE A CD1 
622  C  CD2 . PHE A 84  ? 0.13299 0.15030 0.13405 -0.01004 0.00807  -0.00778 99  PHE A CD2 
623  C  CE1 . PHE A 84  ? 0.16184 0.18119 0.16074 -0.00920 0.01094  -0.00549 99  PHE A CE1 
624  C  CE2 . PHE A 84  ? 0.14039 0.16087 0.14391 -0.01094 0.00888  -0.00627 99  PHE A CE2 
625  C  CZ  . PHE A 84  ? 0.15232 0.17459 0.15538 -0.01026 0.01073  -0.00481 99  PHE A CZ  
626  N  N   . LEU A 85  ? 0.09116 0.10353 0.08886 -0.00380 0.00696  -0.00572 100 LEU A N   
627  C  CA  . LEU A 85  ? 0.13792 0.15306 0.13850 -0.00106 0.00729  -0.00345 100 LEU A CA  
628  C  C   . LEU A 85  ? 0.12320 0.13860 0.12445 -0.00126 0.00552  -0.00188 100 LEU A C   
629  O  O   . LEU A 85  ? 0.13782 0.15785 0.14398 -0.00124 0.00398  0.00071  100 LEU A O   
630  C  CB  . LEU A 85  ? 0.12748 0.13888 0.12434 0.00277  0.00940  -0.00333 100 LEU A CB  
631  C  CG  . LEU A 85  ? 0.15408 0.16901 0.15385 0.00742  0.01117  -0.00005 100 LEU A CG  
632  C  CD1 . LEU A 85  ? 0.17561 0.19961 0.18349 0.00713  0.01163  0.00284  100 LEU A CD1 
633  C  CD2 . LEU A 85  ? 0.18145 0.18937 0.17357 0.01243  0.01376  -0.00072 100 LEU A CD2 
634  N  N   . GLY A 86  ? 0.14300 0.15347 0.13958 -0.00188 0.00514  -0.00279 101 GLY A N   
635  C  CA  . GLY A 86  ? 0.14524 0.15509 0.14122 -0.00224 0.00322  -0.00137 101 GLY A CA  
636  C  C   . GLY A 86  ? 0.14948 0.16074 0.14578 -0.00469 0.00086  -0.00136 101 GLY A C   
637  O  O   . GLY A 86  ? 0.16688 0.17897 0.16442 -0.00501 -0.00201 0.00067  101 GLY A O   
638  N  N   . GLN A 87  ? 0.15704 0.16757 0.15136 -0.00621 0.00160  -0.00341 102 GLN A N   
639  C  CA  . GLN A 87  ? 0.16189 0.17077 0.15350 -0.00756 -0.00072 -0.00387 102 GLN A CA  
640  C  C   . GLN A 87  ? 0.17671 0.18858 0.17331 -0.00844 -0.00380 -0.00212 102 GLN A C   
641  O  O   . GLN A 87  ? 0.19914 0.20858 0.19394 -0.00996 -0.00810 -0.00090 102 GLN A O   
642  C  CB  . GLN A 87  ? 0.15863 0.16619 0.14707 -0.00767 0.00142  -0.00601 102 GLN A CB  
643  C  CG  . GLN A 87  ? 0.17522 0.18160 0.16029 -0.00734 0.00422  -0.00611 102 GLN A CG  
644  C  CD  . GLN A 87  ? 0.28971 0.29198 0.26848 -0.00703 0.00333  -0.00533 102 GLN A CD  
645  O  OE1 . GLN A 87  ? 0.33122 0.33301 0.30921 -0.00728 0.00428  -0.00405 102 GLN A OE1 
646  N  NE2 . GLN A 87  ? 0.30274 0.30056 0.27570 -0.00663 0.00091  -0.00598 102 GLN A NE2 
647  N  N   . CYS A 88  ? 0.20341 0.22014 0.20593 -0.00776 -0.00209 -0.00140 103 CYS A N   
648  C  CA  . CYS A 88  ? 0.19998 0.22154 0.20920 -0.00875 -0.00457 0.00180  103 CYS A CA  
649  C  C   . CYS A 88  ? 0.23356 0.25859 0.24747 -0.00851 -0.00709 0.00598  103 CYS A C   
650  O  O   . CYS A 88  ? 0.25046 0.27680 0.26763 -0.01123 -0.01213 0.00911  103 CYS A O   
651  C  CB  . CYS A 88  ? 0.22845 0.25504 0.24254 -0.00701 -0.00108 0.00253  103 CYS A CB  
652  S  SG  . CYS A 88  ? 0.29005 0.31412 0.30105 -0.00796 0.00037  -0.00096 103 CYS A SG  
653  N  N   . GLN A 89  ? 0.17705 0.20311 0.19130 -0.00536 -0.00422 0.00654  104 GLN A N   
654  C  CA  . GLN A 89  ? 0.17709 0.20755 0.19684 -0.00404 -0.00595 0.01114  104 GLN A CA  
655  C  C   . GLN A 89  ? 0.19081 0.21678 0.20675 -0.00690 -0.01127 0.01153  104 GLN A C   
656  O  O   . GLN A 89  ? 0.21674 0.24685 0.23866 -0.00815 -0.01562 0.01629  104 GLN A O   
657  C  CB  . GLN A 89  ? 0.15344 0.18335 0.17186 0.00088  -0.00153 0.01105  104 GLN A CB  
658  C  CG  . GLN A 89  ? 0.15564 0.18940 0.17690 0.00461  0.00314  0.01183  104 GLN A CG  
659  C  CD  . GLN A 89  ? 0.19703 0.22484 0.21160 0.00942  0.00706  0.00986  104 GLN A CD  
660  O  OE1 . GLN A 89  ? 0.18465 0.20474 0.19213 0.00851  0.00625  0.00687  104 GLN A OE1 
661  N  NE2 . GLN A 89  ? 0.21168 0.24208 0.22743 0.01474  0.01120  0.01186  104 GLN A NE2 
662  N  N   . LEU A 90  ? 0.19579 0.21354 0.20181 -0.00792 -0.01115 0.00721  105 LEU A N   
663  C  CA  . LEU A 90  ? 0.21526 0.22666 0.21452 -0.01015 -0.01595 0.00715  105 LEU A CA  
664  C  C   . LEU A 90  ? 0.24081 0.25072 0.24051 -0.01377 -0.02219 0.00879  105 LEU A C   
665  O  O   . LEU A 90  ? 0.25082 0.25914 0.25058 -0.01603 -0.02842 0.01195  105 LEU A O   
666  C  CB  . LEU A 90  ? 0.20873 0.21257 0.19718 -0.00969 -0.01321 0.00281  105 LEU A CB  
667  C  CG  . LEU A 90  ? 0.31220 0.30817 0.29063 -0.01034 -0.01607 0.00244  105 LEU A CG  
668  C  CD1 . LEU A 90  ? 0.29624 0.29371 0.27735 -0.00975 -0.01790 0.00554  105 LEU A CD1 
669  C  CD2 . LEU A 90  ? 0.30557 0.29722 0.27574 -0.00895 -0.01136 -0.00052 105 LEU A CD2 
670  N  N   . GLU A 91  ? 0.23777 0.24740 0.23755 -0.01473 -0.02146 0.00707  106 GLU A N   
671  C  CA  . GLU A 91  ? 0.23350 0.23980 0.23272 -0.01862 -0.02820 0.00874  106 GLU A CA  
672  C  C   . GLU A 91  ? 0.29834 0.31434 0.31099 -0.02095 -0.03236 0.01573  106 GLU A C   
673  O  O   . GLU A 91  ? 0.29438 0.30723 0.30706 -0.02528 -0.04063 0.01910  106 GLU A O   
674  C  CB  . GLU A 91  ? 0.31329 0.31743 0.31029 -0.01870 -0.02613 0.00574  106 GLU A CB  
675  C  CG  . GLU A 91  ? 0.34508 0.34125 0.33723 -0.02259 -0.03362 0.00637  106 GLU A CG  
676  C  CD  . GLU A 91  ? 0.44455 0.44910 0.44965 -0.02643 -0.03799 0.01252  106 GLU A CD  
677  O  OE1 . GLU A 91  ? 0.37219 0.38932 0.38947 -0.02472 -0.03303 0.01549  106 GLU A OE1 
678  O  OE2 . GLU A 91  ? 0.51388 0.51180 0.51630 -0.03109 -0.04658 0.01485  106 GLU A OE2 
679  N  N   . MET A 92  ? 0.25854 0.28590 0.28214 -0.01793 -0.02695 0.01852  107 MET A N   
680  C  CA  . MET A 92  ? 0.23194 0.27132 0.26999 -0.01849 -0.02884 0.02641  107 MET A CA  
681  C  C   . MET A 92  ? 0.21220 0.25438 0.25378 -0.01783 -0.03173 0.03053  107 MET A C   
682  O  O   . MET A 92  ? 0.24184 0.29551 0.29685 -0.01783 -0.03336 0.03832  107 MET A O   
683  C  CB  . MET A 92  ? 0.26258 0.31154 0.30822 -0.01373 -0.02070 0.02762  107 MET A CB  
684  C  CG  . MET A 92  ? 0.30423 0.35059 0.34647 -0.01433 -0.01798 0.02380  107 MET A CG  
685  S  SD  . MET A 92  ? 0.61172 0.66313 0.65541 -0.00804 -0.00822 0.02235  107 MET A SD  
686  C  CE  . MET A 92  ? 0.36887 0.42763 0.41874 -0.00229 -0.00484 0.02725  107 MET A CE  
687  N  N   . GLU A 93  ? 0.25895 0.29173 0.28944 -0.01701 -0.03216 0.02620  108 GLU A N   
688  C  CA  . GLU A 93  ? 0.23179 0.26539 0.26370 -0.01638 -0.03526 0.02956  108 GLU A CA  
689  C  C   . GLU A 93  ? 0.23843 0.28204 0.27959 -0.01043 -0.02900 0.03290  108 GLU A C   
690  O  O   . GLU A 93  ? 0.26465 0.31396 0.31293 -0.00933 -0.03153 0.03856  108 GLU A O   
691  C  CB  . GLU A 93  ? 0.28927 0.32425 0.32653 -0.02199 -0.04560 0.03592  108 GLU A CB  
692  C  CG  . GLU A 93  ? 0.32475 0.34521 0.34828 -0.02715 -0.05261 0.03192  108 GLU A CG  
693  C  CD  . GLU A 93  ? 0.49975 0.51907 0.52715 -0.03385 -0.06458 0.03831  108 GLU A CD  
694  O  OE1 . GLU A 93  ? 0.49636 0.52524 0.53578 -0.03483 -0.06850 0.04589  108 GLU A OE1 
695  O  OE2 . GLU A 93  ? 0.52242 0.53054 0.54046 -0.03817 -0.07060 0.03608  108 GLU A OE2 
696  N  N   . SER A 94  ? 0.21702 0.26175 0.25708 -0.00617 -0.02108 0.02953  109 SER A N   
697  C  CA  . SER A 94  ? 0.22219 0.27080 0.26485 0.00064  -0.01463 0.03064  109 SER A CA  
698  C  C   . SER A 94  ? 0.20435 0.24173 0.23448 0.00196  -0.01282 0.02475  109 SER A C   
699  O  O   . SER A 94  ? 0.18722 0.21915 0.21041 0.00355  -0.00826 0.01977  109 SER A O   
700  C  CB  . SER A 94  ? 0.24983 0.30315 0.29554 0.00434  -0.00807 0.03031  109 SER A CB  
701  O  OG  . SER A 94  ? 0.35718 0.42230 0.41560 0.00332  -0.00919 0.03706  109 SER A OG  
702  N  N   . TYR A 95  ? 0.20385 0.23778 0.23133 0.00077  -0.01710 0.02602  110 TYR A N   
703  C  CA  . TYR A 95  ? 0.20213 0.22520 0.21735 0.00042  -0.01642 0.02104  110 TYR A CA  
704  C  C   . TYR A 95  ? 0.18835 0.20844 0.20051 0.00561  -0.01103 0.01962  110 TYR A C   
705  O  O   . TYR A 95  ? 0.18997 0.20244 0.19350 0.00504  -0.00861 0.01503  110 TYR A O   
706  C  CB  . TYR A 95  ? 0.19528 0.21450 0.20711 -0.00211 -0.02257 0.02304  110 TYR A CB  
707  C  CG  . TYR A 95  ? 0.21961 0.23714 0.23007 -0.00753 -0.02921 0.02368  110 TYR A CG  
708  C  CD1 . TYR A 95  ? 0.24300 0.25277 0.24353 -0.01013 -0.02902 0.01854  110 TYR A CD1 
709  C  CD2 . TYR A 95  ? 0.26580 0.28871 0.28442 -0.00994 -0.03617 0.02990  110 TYR A CD2 
710  C  CE1 . TYR A 95  ? 0.27049 0.27551 0.26683 -0.01442 -0.03553 0.01872  110 TYR A CE1 
711  C  CE2 . TYR A 95  ? 0.22632 0.24487 0.24175 -0.01550 -0.04374 0.03053  110 TYR A CE2 
712  C  CZ  . TYR A 95  ? 0.25235 0.26068 0.25532 -0.01745 -0.04338 0.02448  110 TYR A CZ  
713  O  OH  . TYR A 95  ? 0.37416 0.37502 0.37106 -0.02234 -0.05135 0.02471  110 TYR A OH  
714  N  N   . ASP A 96  ? 0.19105 0.21636 0.20968 0.01083  -0.00946 0.02402  111 ASP A N   
715  C  CA  . ASP A 96  ? 0.21442 0.23351 0.22720 0.01639  -0.00503 0.02240  111 ASP A CA  
716  C  C   . ASP A 96  ? 0.19843 0.21428 0.20692 0.01787  -0.00032 0.01839  111 ASP A C   
717  O  O   . ASP A 96  ? 0.17565 0.18140 0.17457 0.01850  0.00122  0.01457  111 ASP A O   
718  C  CB  . ASP A 96  ? 0.24183 0.26691 0.26168 0.02327  -0.00358 0.02826  111 ASP A CB  
719  C  CG  . ASP A 96  ? 0.31969 0.34672 0.34303 0.02204  -0.00879 0.03245  111 ASP A CG  
720  O  OD1 . ASP A 96  ? 0.32358 0.34339 0.33969 0.01694  -0.01275 0.02971  111 ASP A OD1 
721  O  OD2 . ASP A 96  ? 0.43908 0.47519 0.47240 0.02657  -0.00876 0.03905  111 ASP A OD2 
722  N  N   . GLU A 97  ? 0.20196 0.22586 0.21732 0.01800  0.00135  0.01974  112 GLU A N   
723  C  CA  . GLU A 97  ? 0.16724 0.18778 0.17798 0.01892  0.00518  0.01599  112 GLU A CA  
724  C  C   . GLU A 97  ? 0.17183 0.18571 0.17575 0.01293  0.00352  0.01071  112 GLU A C   
725  O  O   . GLU A 97  ? 0.16126 0.16765 0.15778 0.01322  0.00533  0.00716  112 GLU A O   
726  C  CB  . GLU A 97  ? 0.21615 0.24720 0.23595 0.01959  0.00696  0.01907  112 GLU A CB  
727  C  CG  . GLU A 97  ? 0.28208 0.32204 0.30987 0.02660  0.01041  0.02544  112 GLU A CG  
728  C  CD  . GLU A 97  ? 0.41281 0.46271 0.44861 0.02685  0.01284  0.02859  112 GLU A CD  
729  O  OE1 . GLU A 97  ? 0.46452 0.52269 0.50974 0.02122  0.00873  0.03176  112 GLU A OE1 
730  O  OE2 . GLU A 97  ? 0.40940 0.45743 0.44078 0.03242  0.01837  0.02787  112 GLU A OE2 
731  N  N   . ALA A 98  ? 0.14945 0.16566 0.15540 0.00771  -0.00014 0.01065  113 ALA A N   
732  C  CA  . ALA A 98  ? 0.14698 0.15823 0.14695 0.00331  -0.00073 0.00654  113 ALA A CA  
733  C  C   . ALA A 98  ? 0.13166 0.13467 0.12376 0.00297  -0.00038 0.00471  113 ALA A C   
734  O  O   . ALA A 98  ? 0.15227 0.15131 0.14021 0.00139  0.00106  0.00214  113 ALA A O   
735  C  CB  . ALA A 98  ? 0.16953 0.18234 0.17027 -0.00073 -0.00465 0.00697  113 ALA A CB  
736  N  N   . ILE A 99  ? 0.11508 0.11578 0.10578 0.00415  -0.00210 0.00676  114 ILE A N   
737  C  CA  . ILE A 99  ? 0.14514 0.13768 0.12854 0.00357  -0.00221 0.00592  114 ILE A CA  
738  C  C   . ILE A 99  ? 0.17355 0.15982 0.15292 0.00616  -0.00017 0.00460  114 ILE A C   
739  O  O   . ILE A 99  ? 0.16351 0.14340 0.13746 0.00349  -0.00038 0.00314  114 ILE A O   
740  C  CB  . ILE A 99  ? 0.16698 0.15811 0.14972 0.00475  -0.00480 0.00877  114 ILE A CB  
741  C  CG1 . ILE A 99  ? 0.17780 0.17142 0.16060 0.00128  -0.00790 0.00948  114 ILE A CG1 
742  C  CG2 . ILE A 99  ? 0.20092 0.18281 0.17621 0.00481  -0.00492 0.00858  114 ILE A CG2 
743  C  CD1 . ILE A 99  ? 0.21884 0.21242 0.20230 0.00211  -0.01164 0.01291  114 ILE A CD1 
744  N  N   . ALA A 100 ? 0.13419 0.12166 0.11555 0.01149  0.00162  0.00561  115 ALA A N   
745  C  CA  . ALA A 100 ? 0.17614 0.15461 0.15029 0.01491  0.00325  0.00396  115 ALA A CA  
746  C  C   . ALA A 100 ? 0.15735 0.13391 0.12916 0.01131  0.00361  0.00098  115 ALA A C   
747  O  O   . ALA A 100 ? 0.16438 0.13091 0.12848 0.00977  0.00225  -0.00062 115 ALA A O   
748  C  CB  . ALA A 100 ? 0.18557 0.16672 0.16177 0.02264  0.00633  0.00605  115 ALA A CB  
749  N  N   . ASN A 101 ? 0.13230 0.11792 0.11073 0.00956  0.00470  0.00065  116 ASN A N   
750  C  CA  . ASN A 101 ? 0.12832 0.11288 0.10530 0.00653  0.00497  -0.00176 116 ASN A CA  
751  C  C   . ASN A 101 ? 0.12927 0.11241 0.10522 0.00070  0.00308  -0.00236 116 ASN A C   
752  O  O   . ASN A 101 ? 0.13103 0.10982 0.10393 -0.00195 0.00218  -0.00336 116 ASN A O   
753  C  CB  . ASN A 101 ? 0.13697 0.13108 0.12108 0.00651  0.00652  -0.00159 116 ASN A CB  
754  C  CG  . ASN A 101 ? 0.16522 0.15977 0.14889 0.01197  0.00931  -0.00089 116 ASN A CG  
755  O  OD1 . ASN A 101 ? 0.16875 0.15553 0.14504 0.01361  0.00999  -0.00274 116 ASN A OD1 
756  N  ND2 . ASN A 101 ? 0.16245 0.16582 0.15361 0.01483  0.01073  0.00239  116 ASN A ND2 
757  N  N   . LEU A 102 ? 0.11988 0.10679 0.09825 -0.00123 0.00240  -0.00113 117 LEU A N   
758  C  CA  . LEU A 102 ? 0.13006 0.11635 0.10711 -0.00559 0.00178  -0.00065 117 LEU A CA  
759  C  C   . LEU A 102 ? 0.14871 0.12633 0.12032 -0.00704 -0.00003 0.00050  117 LEU A C   
760  O  O   . LEU A 102 ? 0.14861 0.12502 0.11988 -0.01103 -0.00082 0.00146  117 LEU A O   
761  C  CB  . LEU A 102 ? 0.14365 0.13390 0.12165 -0.00626 0.00169  0.00038  117 LEU A CB  
762  C  CG  . LEU A 102 ? 0.13244 0.12879 0.11402 -0.00611 0.00224  -0.00069 117 LEU A CG  
763  C  CD1 . LEU A 102 ? 0.15074 0.14722 0.13010 -0.00628 0.00065  0.00023  117 LEU A CD1 
764  C  CD2 . LEU A 102 ? 0.13138 0.13032 0.11401 -0.00802 0.00399  -0.00175 117 LEU A CD2 
765  N  N   . GLN A 103 ? 0.14838 0.11983 0.11604 -0.00396 -0.00110 0.00106  118 GLN A N   
766  C  CA  . GLN A 103 ? 0.16831 0.12883 0.12912 -0.00521 -0.00366 0.00203  118 GLN A CA  
767  C  C   . GLN A 103 ? 0.15878 0.11133 0.11473 -0.00559 -0.00518 0.00046  118 GLN A C   
768  O  O   . GLN A 103 ? 0.18910 0.13419 0.14107 -0.00994 -0.00849 0.00167  118 GLN A O   
769  C  CB  . GLN A 103 ? 0.20261 0.15725 0.15938 -0.00061 -0.00436 0.00285  118 GLN A CB  
770  C  CG  . GLN A 103 ? 0.21300 0.17242 0.17239 -0.00119 -0.00453 0.00499  118 GLN A CG  
771  C  CD  . GLN A 103 ? 0.35670 0.31251 0.31417 0.00414  -0.00517 0.00622  118 GLN A CD  
772  O  OE1 . GLN A 103 ? 0.33627 0.29158 0.29399 0.00971  -0.00377 0.00570  118 GLN A OE1 
773  N  NE2 . GLN A 103 ? 0.32384 0.27761 0.27946 0.00299  -0.00693 0.00844  118 GLN A NE2 
774  N  N   . ARG A 104 ? 0.14555 0.09933 0.10151 -0.00144 -0.00325 -0.00169 119 ARG A N   
775  C  CA  . ARG A 104 ? 0.17759 0.12248 0.12690 -0.00150 -0.00494 -0.00342 119 ARG A CA  
776  C  C   . ARG A 104 ? 0.17992 0.12957 0.13390 -0.00805 -0.00645 -0.00290 119 ARG A C   
777  O  O   . ARG A 104 ? 0.17236 0.11309 0.12113 -0.01177 -0.01056 -0.00248 119 ARG A O   
778  C  CB  . ARG A 104 ? 0.17608 0.12223 0.12417 0.00510  -0.00161 -0.00520 119 ARG A CB  
779  C  CG  . ARG A 104 ? 0.16505 0.10026 0.10358 0.00604  -0.00320 -0.00730 119 ARG A CG  
780  C  CD  . ARG A 104 ? 0.20682 0.12270 0.13083 0.00731  -0.00726 -0.00790 119 ARG A CD  
781  N  NE  . ARG A 104 ? 0.19510 0.09781 0.10671 0.00965  -0.00896 -0.01025 119 ARG A NE  
782  C  CZ  . ARG A 104 ? 0.22798 0.11097 0.12488 0.00832  -0.01476 -0.01119 119 ARG A CZ  
783  N  NH1 . ARG A 104 ? 0.27084 0.14513 0.16415 0.00468  -0.01931 -0.00967 119 ARG A NH1 
784  N  NH2 . ARG A 104 ? 0.22693 0.09738 0.11136 0.01036  -0.01670 -0.01350 119 ARG A NH2 
785  N  N   . ALA A 105 ? 0.13830 0.10134 0.10175 -0.00944 -0.00366 -0.00251 120 ALA A N   
786  C  CA  . ALA A 105 ? 0.14955 0.11853 0.11843 -0.01470 -0.00435 -0.00115 120 ALA A CA  
787  C  C   . ALA A 105 ? 0.13920 0.10598 0.10832 -0.01999 -0.00706 0.00254  120 ALA A C   
788  O  O   . ALA A 105 ? 0.16526 0.13096 0.13579 -0.02482 -0.01008 0.00474  120 ALA A O   
789  C  CB  . ALA A 105 ? 0.13413 0.11577 0.11095 -0.01408 -0.00064 -0.00133 120 ALA A CB  
790  N  N   . TYR A 106 ? 0.13619 0.10266 0.10444 -0.01946 -0.00640 0.00402  121 TYR A N   
791  C  CA  . TYR A 106 ? 0.16359 0.12832 0.13216 -0.02448 -0.00868 0.00841  121 TYR A CA  
792  C  C   . TYR A 106 ? 0.17938 0.13027 0.14089 -0.02771 -0.01467 0.00932  121 TYR A C   
793  O  O   . TYR A 106 ? 0.19389 0.14477 0.15827 -0.03402 -0.01814 0.01349  121 TYR A O   
794  C  CB  . TYR A 106 ? 0.16473 0.12940 0.13148 -0.02267 -0.00723 0.00947  121 TYR A CB  
795  C  CG  . TYR A 106 ? 0.25011 0.21355 0.21711 -0.02761 -0.00901 0.01465  121 TYR A CG  
796  C  CD1 . TYR A 106 ? 0.26236 0.23688 0.23582 -0.02997 -0.00581 0.01861  121 TYR A CD1 
797  C  CD2 . TYR A 106 ? 0.30270 0.25337 0.26285 -0.02951 -0.01372 0.01608  121 TYR A CD2 
798  C  CE1 . TYR A 106 ? 0.33255 0.30747 0.30710 -0.03435 -0.00677 0.02453  121 TYR A CE1 
799  C  CE2 . TYR A 106 ? 0.32707 0.27682 0.28803 -0.03472 -0.01573 0.02167  121 TYR A CE2 
800  C  CZ  . TYR A 106 ? 0.36926 0.33215 0.33818 -0.03727 -0.01200 0.02624  121 TYR A CZ  
801  O  OH  . TYR A 106 ? 0.44788 0.41128 0.41844 -0.04236 -0.01338 0.03300  121 TYR A OH  
802  N  N   . SER A 107 ? 0.18472 0.12321 0.13652 -0.02319 -0.01620 0.00593  122 SER A N   
803  C  CA  . SER A 107 ? 0.18374 0.10472 0.12469 -0.02512 -0.02247 0.00600  122 SER A CA  
804  C  C   . SER A 107 ? 0.21485 0.13296 0.15508 -0.02891 -0.02615 0.00584  122 SER A C   
805  O  O   . SER A 107 ? 0.25694 0.16538 0.19330 -0.03520 -0.03299 0.00875  122 SER A O   
806  C  CB  . SER A 107 ? 0.26111 0.16952 0.19055 -0.01718 -0.02187 0.00217  122 SER A CB  
807  O  OG  . SER A 107 ? 0.36890 0.27608 0.29741 -0.01513 -0.02096 0.00351  122 SER A OG  
808  N  N   . LEU A 108 ? 0.18209 0.10780 0.12574 -0.02557 -0.02246 0.00289  123 LEU A N   
809  C  CA  . LEU A 108 ? 0.20101 0.12419 0.14374 -0.02882 -0.02601 0.00268  123 LEU A CA  
810  C  C   . LEU A 108 ? 0.20327 0.13796 0.15818 -0.03676 -0.02793 0.00809  123 LEU A C   
811  O  O   . LEU A 108 ? 0.23079 0.15964 0.18445 -0.04269 -0.03446 0.01067  123 LEU A O   
812  C  CB  . LEU A 108 ? 0.18598 0.11560 0.13013 -0.02318 -0.02109 -0.00122 123 LEU A CB  
813  C  CG  . LEU A 108 ? 0.21081 0.13047 0.14369 -0.01479 -0.01873 -0.00539 123 LEU A CG  
814  C  CD1 . LEU A 108 ? 0.21195 0.14381 0.15132 -0.01034 -0.01285 -0.00733 123 LEU A CD1 
815  C  CD2 . LEU A 108 ? 0.27151 0.17093 0.18827 -0.01441 -0.02444 -0.00713 123 LEU A CD2 
816  N  N   . ALA A 109 ? 0.19391 0.14473 0.16026 -0.03666 -0.02246 0.01038  124 ALA A N   
817  C  CA  . ALA A 109 ? 0.18526 0.14863 0.16361 -0.04260 -0.02269 0.01647  124 ALA A CA  
818  C  C   . ALA A 109 ? 0.23027 0.18744 0.20823 -0.04974 -0.02884 0.02250  124 ALA A C   
819  O  O   . ALA A 109 ? 0.23152 0.19268 0.21652 -0.05648 -0.03319 0.02823  124 ALA A O   
820  C  CB  . ALA A 109 ? 0.19990 0.17875 0.18674 -0.03934 -0.01501 0.01728  124 ALA A CB  
821  N  N   . LYS A 110 ? 0.21505 0.16248 0.18532 -0.04868 -0.02982 0.02197  125 LYS A N   
822  C  CA  . LYS A 110 ? 0.23716 0.17599 0.20538 -0.05578 -0.03663 0.02770  125 LYS A CA  
823  C  C   . LYS A 110 ? 0.26766 0.18932 0.22669 -0.06045 -0.04635 0.02752  125 LYS A C   
824  O  O   . LYS A 110 ? 0.24641 0.16747 0.21023 -0.06926 -0.05327 0.03436  125 LYS A O   
825  C  CB  . LYS A 110 ? 0.24546 0.17546 0.20551 -0.05257 -0.03570 0.02629  125 LYS A CB  
826  C  CG  . LYS A 110 ? 0.31647 0.23526 0.27264 -0.05960 -0.04303 0.03202  125 LYS A CG  
827  C  CD  . LYS A 110 ? 0.36840 0.27946 0.31677 -0.05535 -0.04129 0.03035  125 LYS A CD  
828  C  CE  . LYS A 110 ? 0.41263 0.31334 0.35778 -0.06262 -0.04827 0.03674  125 LYS A CE  
829  N  NZ  . LYS A 110 ? 0.38308 0.27254 0.31805 -0.05775 -0.04767 0.03432  125 LYS A NZ  
830  N  N   . GLU A 111 ? 0.26209 0.16945 0.20750 -0.05457 -0.04718 0.02030  126 GLU A N   
831  C  CA  . GLU A 111 ? 0.32509 0.21266 0.25747 -0.05755 -0.05637 0.01901  126 GLU A CA  
832  C  C   . GLU A 111 ? 0.31879 0.21474 0.26034 -0.06380 -0.06007 0.02254  126 GLU A C   
833  O  O   . GLU A 111 ? 0.35920 0.24322 0.29620 -0.07153 -0.07038 0.02621  126 GLU A O   
834  C  CB  . GLU A 111 ? 0.32304 0.19675 0.23946 -0.04766 -0.05372 0.01069  126 GLU A CB  
835  C  CG  . GLU A 111 ? 0.47480 0.32532 0.37317 -0.04796 -0.06183 0.00781  126 GLU A CG  
836  C  CD  . GLU A 111 ? 0.54444 0.38657 0.42965 -0.03645 -0.05625 0.00046  126 GLU A CD  
837  O  OE1 . GLU A 111 ? 0.55970 0.41027 0.44827 -0.02892 -0.04789 -0.00173 126 GLU A OE1 
838  O  OE2 . GLU A 111 ? 0.62260 0.45021 0.49432 -0.03487 -0.06021 -0.00251 126 GLU A OE2 
839  N  N   . GLN A 112 ? 0.27054 0.18638 0.22498 -0.06088 -0.05253 0.02202  127 GLN A N   
840  C  CA  . GLN A 112 ? 0.25777 0.18315 0.22180 -0.06544 -0.05502 0.02527  127 GLN A CA  
841  C  C   . GLN A 112 ? 0.27443 0.21879 0.25746 -0.07247 -0.05485 0.03487  127 GLN A C   
842  O  O   . GLN A 112 ? 0.30831 0.26348 0.30205 -0.07611 -0.05646 0.03898  127 GLN A O   
843  C  CB  . GLN A 112 ? 0.25245 0.18783 0.21923 -0.05802 -0.04720 0.01976  127 GLN A CB  
844  C  CG  . GLN A 112 ? 0.25411 0.17258 0.20363 -0.05156 -0.04768 0.01199  127 GLN A CG  
845  C  CD  . GLN A 112 ? 0.22473 0.15420 0.17773 -0.04365 -0.03866 0.00713  127 GLN A CD  
846  O  OE1 . GLN A 112 ? 0.23991 0.18597 0.20590 -0.04427 -0.03492 0.00890  127 GLN A OE1 
847  N  NE2 . GLN A 112 ? 0.22218 0.14247 0.16377 -0.03602 -0.03519 0.00162  127 GLN A NE2 
848  N  N   . ARG A 113 ? 0.26755 0.21657 0.25504 -0.07400 -0.05267 0.03909  128 ARG A N   
849  C  CA  . ARG A 113 ? 0.26616 0.23395 0.27137 -0.07969 -0.05121 0.04929  128 ARG A CA  
850  C  C   . ARG A 113 ? 0.27871 0.26842 0.29750 -0.07497 -0.04195 0.05000  128 ARG A C   
851  O  O   . ARG A 113 ? 0.31084 0.31561 0.34439 -0.07923 -0.04231 0.05805  128 ARG A O   
852  C  CB  . ARG A 113 ? 0.34396 0.30777 0.35392 -0.09097 -0.06276 0.05801  128 ARG A CB  
853  N  N   . LEU A 114 ? 0.21956 0.21067 0.23326 -0.06599 -0.03395 0.04201  129 LEU A N   
854  C  CA  . LEU A 114 ? 0.25844 0.26660 0.28147 -0.06052 -0.02531 0.04144  129 LEU A CA  
855  C  C   . LEU A 114 ? 0.26506 0.28474 0.29337 -0.05745 -0.01746 0.04475  129 LEU A C   
856  O  O   . LEU A 114 ? 0.32464 0.33705 0.34543 -0.05605 -0.01656 0.04280  129 LEU A O   
857  C  CB  . LEU A 114 ? 0.30020 0.30276 0.31447 -0.05317 -0.02187 0.03168  129 LEU A CB  
858  C  CG  . LEU A 114 ? 0.24004 0.23172 0.24755 -0.05432 -0.02789 0.02783  129 LEU A CG  
859  C  CD1 . LEU A 114 ? 0.22238 0.21249 0.22389 -0.04668 -0.02281 0.01980  129 LEU A CD1 
860  C  CD2 . LEU A 114 ? 0.31143 0.31253 0.33019 -0.05952 -0.03143 0.03398  129 LEU A CD2 
861  N  N   . ASN A 115 ? 0.24750 0.28439 0.28759 -0.05565 -0.01158 0.04975  130 ASN A N   
862  C  CA  . ASN A 115 ? 0.27206 0.31991 0.31597 -0.05187 -0.00347 0.05368  130 ASN A CA  
863  C  C   . ASN A 115 ? 0.25232 0.30518 0.29362 -0.04296 0.00453  0.04788  130 ASN A C   
864  O  O   . ASN A 115 ? 0.28766 0.35003 0.33616 -0.04079 0.00711  0.04931  130 ASN A O   
865  C  CB  . ASN A 115 ? 0.31036 0.37405 0.36943 -0.05633 -0.00259 0.06603  130 ASN A CB  
866  C  CG  . ASN A 115 ? 0.35960 0.43380 0.42086 -0.05173 0.00645  0.07087  130 ASN A CG  
867  O  OD1 . ASN A 115 ? 0.33952 0.40607 0.38976 -0.04757 0.00960  0.06560  130 ASN A OD1 
868  N  ND2 . ASN A 115 ? 0.37636 0.46827 0.45165 -0.05209 0.01073  0.08149  130 ASN A ND2 
869  N  N   . PHE A 116 ? 0.24510 0.29095 0.27596 -0.03803 0.00779  0.04178  131 PHE A N   
870  C  CA  . PHE A 116 ? 0.23998 0.28868 0.26674 -0.03023 0.01446  0.03708  131 PHE A CA  
871  C  C   . PHE A 116 ? 0.24123 0.29261 0.26391 -0.02642 0.02039  0.03953  131 PHE A C   
872  O  O   . PHE A 116 ? 0.21718 0.26389 0.23082 -0.02086 0.02351  0.03411  131 PHE A O   
873  C  CB  . PHE A 116 ? 0.24188 0.27955 0.25940 -0.02756 0.01231  0.02768  131 PHE A CB  
874  C  CG  . PHE A 116 ? 0.23990 0.27416 0.25924 -0.03001 0.00747  0.02499  131 PHE A CG  
875  C  CD1 . PHE A 116 ? 0.24164 0.28350 0.26749 -0.02893 0.00878  0.02587  131 PHE A CD1 
876  C  CD2 . PHE A 116 ? 0.27216 0.29468 0.28542 -0.03272 0.00176  0.02171  131 PHE A CD2 
877  C  CE1 . PHE A 116 ? 0.25489 0.29283 0.28124 -0.03119 0.00410  0.02352  131 PHE A CE1 
878  C  CE2 . PHE A 116 ? 0.24923 0.26702 0.26169 -0.03426 -0.00245 0.01920  131 PHE A CE2 
879  C  CZ  . PHE A 116 ? 0.21416 0.23972 0.23320 -0.03384 -0.00148 0.02009  131 PHE A CZ  
880  N  N   . GLY A 117 ? 0.23231 0.29084 0.26119 -0.02962 0.02158  0.04822  132 GLY A N   
881  C  CA  . GLY A 117 ? 0.18307 0.24310 0.20658 -0.02600 0.02724  0.05098  132 GLY A CA  
882  C  C   . GLY A 117 ? 0.21716 0.26342 0.22851 -0.02568 0.02425  0.04452  132 GLY A C   
883  O  O   . GLY A 117 ? 0.20933 0.24682 0.21923 -0.03035 0.01764  0.04209  132 GLY A O   
884  N  N   . ASP A 118 ? 0.18537 0.22876 0.18690 -0.01962 0.02893  0.04177  133 ASP A N   
885  C  CA  . ASP A 118 ? 0.19240 0.22393 0.18311 -0.01893 0.02605  0.03640  133 ASP A CA  
886  C  C   . ASP A 118 ? 0.16756 0.19210 0.15240 -0.01560 0.02406  0.02765  133 ASP A C   
887  O  O   . ASP A 118 ? 0.16889 0.18544 0.14489 -0.01361 0.02261  0.02370  133 ASP A O   
888  C  CB  . ASP A 118 ? 0.17578 0.20685 0.15823 -0.01529 0.03088  0.03939  133 ASP A CB  
889  C  CG  . ASP A 118 ? 0.25165 0.27208 0.22573 -0.01668 0.02685  0.03694  133 ASP A CG  
890  O  OD1 . ASP A 118 ? 0.27110 0.28779 0.24875 -0.02204 0.02159  0.03789  133 ASP A OD1 
891  O  OD2 . ASP A 118 ? 0.25516 0.26999 0.21820 -0.01224 0.02857  0.03431  133 ASP A OD2 
892  N  N   . ASP A 119 ? 0.17301 0.20071 0.16334 -0.01548 0.02339  0.02526  134 ASP A N   
893  C  CA  . ASP A 119 ? 0.17644 0.19905 0.16203 -0.01226 0.02216  0.01821  134 ASP A CA  
894  C  C   . ASP A 119 ? 0.15128 0.16534 0.13339 -0.01385 0.01701  0.01394  134 ASP A C   
895  O  O   . ASP A 119 ? 0.13889 0.14795 0.11477 -0.01118 0.01609  0.01010  134 ASP A O   
896  C  CB  . ASP A 119 ? 0.16292 0.19058 0.15554 -0.01235 0.02215  0.01719  134 ASP A CB  
897  C  CG  . ASP A 119 ? 0.19188 0.22710 0.18611 -0.00812 0.02793  0.02006  134 ASP A CG  
898  O  OD1 . ASP A 119 ? 0.19701 0.23338 0.18609 -0.00464 0.03253  0.02299  134 ASP A OD1 
899  O  OD2 . ASP A 119 ? 0.21134 0.25093 0.21116 -0.00756 0.02819  0.01956  134 ASP A OD2 
900  N  N   . ILE A 120 ? 0.15036 0.16209 0.13599 -0.01791 0.01332  0.01497  135 ILE A N   
901  C  CA  . ILE A 120 ? 0.14298 0.14682 0.12509 -0.01775 0.00939  0.01109  135 ILE A CA  
902  C  C   . ILE A 120 ? 0.14840 0.14728 0.12432 -0.01684 0.00879  0.01172  135 ILE A C   
903  O  O   . ILE A 120 ? 0.13942 0.13489 0.11185 -0.01430 0.00747  0.00859  135 ILE A O   
904  C  CB  . ILE A 120 ? 0.13485 0.13442 0.11914 -0.02109 0.00549  0.01136  135 ILE A CB  
905  C  CG1 . ILE A 120 ? 0.15217 0.15619 0.14184 -0.02204 0.00551  0.01076  135 ILE A CG1 
906  C  CG2 . ILE A 120 ? 0.13953 0.13117 0.11917 -0.01886 0.00289  0.00761  135 ILE A CG2 
907  C  CD1 . ILE A 120 ? 0.17242 0.16996 0.16180 -0.02547 0.00076  0.01095  135 ILE A CD1 
908  N  N   . PRO A 121 ? 0.14888 0.14763 0.12375 -0.01900 0.00938  0.01632  136 PRO A N   
909  C  CA  . PRO A 121 ? 0.14896 0.14280 0.11695 -0.01771 0.00892  0.01688  136 PRO A CA  
910  C  C   . PRO A 121 ? 0.16698 0.16110 0.12906 -0.01369 0.01107  0.01477  136 PRO A C   
911  O  O   . PRO A 121 ? 0.16642 0.15520 0.12322 -0.01222 0.00858  0.01302  136 PRO A O   
912  C  CB  . PRO A 121 ? 0.17758 0.17325 0.14634 -0.02092 0.01020  0.02325  136 PRO A CB  
913  C  CG  . PRO A 121 ? 0.18360 0.18130 0.15974 -0.02528 0.00816  0.02550  136 PRO A CG  
914  C  CD  . PRO A 121 ? 0.17020 0.17240 0.15044 -0.02349 0.00926  0.02184  136 PRO A CD  
915  N  N   . SER A 122 ? 0.16529 0.16456 0.12744 -0.01172 0.01514  0.01514  137 SER A N   
916  C  CA  . SER A 122 ? 0.17243 0.16861 0.12596 -0.00759 0.01638  0.01265  137 SER A CA  
917  C  C   . SER A 122 ? 0.15803 0.15054 0.11136 -0.00695 0.01213  0.00774  137 SER A C   
918  O  O   . SER A 122 ? 0.15244 0.13909 0.09840 -0.00552 0.00947  0.00612  137 SER A O   
919  C  CB  . SER A 122 ? 0.18304 0.18429 0.13602 -0.00454 0.02179  0.01386  137 SER A CB  
920  O  OG  . SER A 122 ? 0.20562 0.21111 0.15753 -0.00380 0.02672  0.01962  137 SER A OG  
921  N  N   . ALA A 123 ? 0.15272 0.14867 0.11415 -0.00825 0.01107  0.00597  138 ALA A N   
922  C  CA  . ALA A 123 ? 0.16620 0.16053 0.12924 -0.00777 0.00758  0.00263  138 ALA A CA  
923  C  C   . ALA A 123 ? 0.14739 0.13835 0.11045 -0.00826 0.00389  0.00297  138 ALA A C   
924  O  O   . ALA A 123 ? 0.15671 0.14603 0.11898 -0.00750 0.00067  0.00195  138 ALA A O   
925  C  CB  . ALA A 123 ? 0.15245 0.15116 0.12327 -0.00862 0.00802  0.00130  138 ALA A CB  
926  N  N   . LEU A 124 ? 0.16423 0.15400 0.12854 -0.00959 0.00387  0.00496  139 LEU A N   
927  C  CA  . LEU A 124 ? 0.15896 0.14480 0.12241 -0.00906 0.00078  0.00567  139 LEU A CA  
928  C  C   . LEU A 124 ? 0.16767 0.15008 0.12442 -0.00837 -0.00100 0.00673  139 LEU A C   
929  O  O   . LEU A 124 ? 0.16783 0.14887 0.12495 -0.00738 -0.00451 0.00685  139 LEU A O   
930  C  CB  . LEU A 124 ? 0.16231 0.14488 0.12589 -0.01063 0.00067  0.00766  139 LEU A CB  
931  C  CG  . LEU A 124 ? 0.19408 0.17566 0.16152 -0.01044 0.00009  0.00622  139 LEU A CG  
932  C  CD1 . LEU A 124 ? 0.18159 0.15807 0.14742 -0.01329 -0.00085 0.00828  139 LEU A CD1 
933  C  CD2 . LEU A 124 ? 0.19644 0.17601 0.16452 -0.00691 -0.00173 0.00538  139 LEU A CD2 
934  N  N   . ARG A 125 ? 0.16795 0.14907 0.11842 -0.00866 0.00138  0.00814  140 ARG A N   
935  C  CA  . ARG A 125 ? 0.17977 0.15563 0.12096 -0.00767 -0.00037 0.00899  140 ARG A CA  
936  C  C   . ARG A 125 ? 0.17981 0.15351 0.11775 -0.00657 -0.00356 0.00652  140 ARG A C   
937  O  O   . ARG A 125 ? 0.17932 0.14890 0.11382 -0.00665 -0.00842 0.00700  140 ARG A O   
938  C  CB  . ARG A 125 ? 0.20178 0.17694 0.13591 -0.00718 0.00413  0.01142  140 ARG A CB  
939  C  CG  . ARG A 125 ? 0.32086 0.28902 0.24181 -0.00505 0.00333  0.01163  140 ARG A CG  
940  C  CD  . ARG A 125 ? 0.37030 0.33360 0.28707 -0.00596 0.00020  0.01404  140 ARG A CD  
941  N  NE  . ARG A 125 ? 0.46012 0.41754 0.36321 -0.00402 0.00215  0.01600  140 ARG A NE  
942  C  CZ  . ARG A 125 ? 0.44523 0.39992 0.34394 -0.00471 0.00240  0.01965  140 ARG A CZ  
943  N  NH1 . ARG A 125 ? 0.46047 0.41685 0.36706 -0.00738 0.00041  0.02159  140 ARG A NH1 
944  N  NH2 . ARG A 125 ? 0.51308 0.46202 0.39780 -0.00224 0.00472  0.02149  140 ARG A NH2 
945  N  N   . ILE A 126 ? 0.16788 0.14398 0.10723 -0.00594 -0.00169 0.00432  141 ILE A N   
946  C  CA  . ILE A 126 ? 0.17174 0.14472 0.10835 -0.00568 -0.00574 0.00223  141 ILE A CA  
947  C  C   . ILE A 126 ? 0.17480 0.15087 0.12039 -0.00719 -0.01072 0.00294  141 ILE A C   
948  O  O   . ILE A 126 ? 0.18160 0.15406 0.12456 -0.00808 -0.01651 0.00369  141 ILE A O   
949  C  CB  . ILE A 126 ? 0.17136 0.14661 0.10919 -0.00467 -0.00270 -0.00002 141 ILE A CB  
950  C  CG1 . ILE A 126 ? 0.17837 0.14963 0.10527 -0.00168 0.00190  -0.00005 141 ILE A CG1 
951  C  CG2 . ILE A 126 ? 0.18797 0.16092 0.12637 -0.00557 -0.00787 -0.00170 141 ILE A CG2 
952  C  CD1 . ILE A 126 ? 0.20785 0.18303 0.13753 0.00007  0.00616  -0.00132 141 ILE A CD1 
953  N  N   . ALA A 127 ? 0.16213 0.14476 0.11816 -0.00726 -0.00871 0.00330  142 ALA A N   
954  C  CA  . ALA A 127 ? 0.15159 0.13854 0.11655 -0.00724 -0.01185 0.00470  142 ALA A CA  
955  C  C   . ALA A 127 ? 0.16230 0.14728 0.12656 -0.00697 -0.01568 0.00763  142 ALA A C   
956  O  O   . ALA A 127 ? 0.15913 0.14655 0.12818 -0.00740 -0.02034 0.00993  142 ALA A O   
957  C  CB  . ALA A 127 ? 0.18149 0.17343 0.15430 -0.00608 -0.00823 0.00432  142 ALA A CB  
958  N  N   . LYS A 128 ? 0.17826 0.15938 0.13746 -0.00650 -0.01412 0.00835  143 LYS A N   
959  C  CA  . LYS A 128 ? 0.18351 0.16225 0.14168 -0.00598 -0.01781 0.01128  143 LYS A CA  
960  C  C   . LYS A 128 ? 0.19618 0.16955 0.14626 -0.00747 -0.02308 0.01208  143 LYS A C   
961  O  O   . LYS A 128 ? 0.20874 0.18234 0.16128 -0.00774 -0.02846 0.01506  143 LYS A O   
962  C  CB  . LYS A 128 ? 0.18335 0.15817 0.13743 -0.00549 -0.01515 0.01208  143 LYS A CB  
963  C  CG  . LYS A 128 ? 0.21014 0.18695 0.16999 -0.00424 -0.01179 0.01149  143 LYS A CG  
964  C  CD  . LYS A 128 ? 0.24169 0.21290 0.19662 -0.00496 -0.01038 0.01267  143 LYS A CD  
965  C  CE  . LYS A 128 ? 0.37152 0.34144 0.32953 -0.00419 -0.00850 0.01185  143 LYS A CE  
966  N  NZ  . LYS A 128 ? 0.49557 0.45904 0.44865 -0.00635 -0.00820 0.01348  143 LYS A NZ  
967  N  N   . LYS A 129 ? 0.19040 0.15838 0.13029 -0.00807 -0.02184 0.00980  144 LYS A N   
968  C  CA  . LYS A 129 ? 0.19343 0.15285 0.12186 -0.00906 -0.02750 0.00993  144 LYS A CA  
969  C  C   . LYS A 129 ? 0.20300 0.16426 0.13726 -0.01115 -0.03400 0.01063  144 LYS A C   
970  O  O   . LYS A 129 ? 0.23116 0.18757 0.16151 -0.01299 -0.04151 0.01284  144 LYS A O   
971  C  CB  . LYS A 129 ? 0.21487 0.16707 0.12951 -0.00769 -0.02378 0.00721  144 LYS A CB  
972  C  CG  . LYS A 129 ? 0.31817 0.26704 0.22405 -0.00600 -0.01883 0.00826  144 LYS A CG  
973  C  CD  . LYS A 129 ? 0.35725 0.30386 0.25438 -0.00341 -0.01241 0.00661  144 LYS A CD  
974  C  CE  . LYS A 129 ? 0.43410 0.37650 0.32005 -0.00137 -0.00803 0.00888  144 LYS A CE  
975  N  NZ  . LYS A 129 ? 0.48376 0.42090 0.35648 0.00274  -0.00305 0.00776  144 LYS A NZ  
976  N  N   . LYS A 130 ? 0.21530 0.18262 0.15766 -0.01128 -0.03155 0.00912  145 LYS A N   
977  C  CA  . LYS A 130 ? 0.23407 0.20402 0.18313 -0.01383 -0.03767 0.01076  145 LYS A CA  
978  C  C   . LYS A 130 ? 0.21961 0.19861 0.18254 -0.01435 -0.04121 0.01596  145 LYS A C   
979  O  O   . LYS A 130 ? 0.24462 0.22395 0.21087 -0.01732 -0.04915 0.01967  145 LYS A O   
980  C  CB  . LYS A 130 ? 0.22923 0.20422 0.18433 -0.01364 -0.03377 0.00847  145 LYS A CB  
981  C  CG  . LYS A 130 ? 0.27646 0.24302 0.21885 -0.01269 -0.03112 0.00415  145 LYS A CG  
982  C  CD  . LYS A 130 ? 0.35018 0.30324 0.27751 -0.01412 -0.03832 0.00361  145 LYS A CD  
983  C  CE  . LYS A 130 ? 0.37636 0.32925 0.30910 -0.01829 -0.04703 0.00596  145 LYS A CE  
984  N  NZ  . LYS A 130 ? 0.44185 0.37965 0.35915 -0.02061 -0.05645 0.00629  145 LYS A NZ  
985  N  N   . ARG A 131 ? 0.19616 0.18214 0.16706 -0.01132 -0.03574 0.01684  146 ARG A N   
986  C  CA  . ARG A 131 ? 0.20293 0.19696 0.18569 -0.01002 -0.03801 0.02215  146 ARG A CA  
987  C  C   . ARG A 131 ? 0.22221 0.21105 0.19990 -0.01153 -0.04499 0.02534  146 ARG A C   
988  O  O   . ARG A 131 ? 0.21202 0.20602 0.19820 -0.01318 -0.05158 0.03078  146 ARG A O   
989  C  CB  . ARG A 131 ? 0.20306 0.20085 0.19017 -0.00553 -0.03095 0.02166  146 ARG A CB  
990  C  CG  . ARG A 131 ? 0.24051 0.24611 0.23883 -0.00216 -0.03183 0.02720  146 ARG A CG  
991  C  CD  . ARG A 131 ? 0.29620 0.30183 0.29530 0.00307  -0.02514 0.02605  146 ARG A CD  
992  N  NE  . ARG A 131 ? 0.38332 0.37905 0.37129 0.00302  -0.02388 0.02337  146 ARG A NE  
993  C  CZ  . ARG A 131 ? 0.41103 0.40265 0.39606 0.00622  -0.01956 0.02190  146 ARG A CZ  
994  N  NH1 . ARG A 131 ? 0.41242 0.40740 0.40271 0.01067  -0.01572 0.02214  146 ARG A NH1 
995  N  NH2 . ARG A 131 ? 0.44646 0.42939 0.42200 0.00493  -0.01938 0.02049  146 ARG A NH2 
996  N  N   . TRP A 132 ? 0.20317 0.18226 0.16739 -0.01115 -0.04386 0.02276  147 TRP A N   
997  C  CA  . TRP A 132 ? 0.22223 0.19464 0.17916 -0.01253 -0.05060 0.02549  147 TRP A CA  
998  C  C   . TRP A 132 ? 0.21903 0.18504 0.16974 -0.01686 -0.05975 0.02641  147 TRP A C   
999  O  O   . TRP A 132 ? 0.25022 0.21627 0.20374 -0.01916 -0.06822 0.03130  147 TRP A O   
1000 C  CB  . TRP A 132 ? 0.21924 0.18219 0.16175 -0.01118 -0.04669 0.02268  147 TRP A CB  
1001 C  CG  . TRP A 132 ? 0.25458 0.20852 0.18623 -0.01247 -0.05333 0.02496  147 TRP A CG  
1002 C  CD1 . TRP A 132 ? 0.28299 0.22407 0.19617 -0.01351 -0.05553 0.02278  147 TRP A CD1 
1003 C  CD2 . TRP A 132 ? 0.26257 0.21896 0.20007 -0.01231 -0.05870 0.03010  147 TRP A CD2 
1004 N  NE1 . TRP A 132 ? 0.30538 0.24002 0.21177 -0.01452 -0.06239 0.02602  147 TRP A NE1 
1005 C  CE2 . TRP A 132 ? 0.26278 0.20717 0.18471 -0.01407 -0.06466 0.03068  147 TRP A CE2 
1006 C  CE3 . TRP A 132 ? 0.27214 0.23934 0.22578 -0.01008 -0.05873 0.03455  147 TRP A CE3 
1007 C  CZ2 . TRP A 132 ? 0.32341 0.26680 0.24650 -0.01453 -0.07138 0.03561  147 TRP A CZ2 
1008 C  CZ3 . TRP A 132 ? 0.30596 0.27289 0.26144 -0.00987 -0.06480 0.03968  147 TRP A CZ3 
1009 C  CH2 . TRP A 132 ? 0.34575 0.30112 0.28658 -0.01250 -0.07140 0.04020  147 TRP A CH2 
1010 N  N   . ASN A 133 ? 0.20530 0.16494 0.14716 -0.01806 -0.05886 0.02211  148 ASN A N   
1011 C  CA  . ASN A 133 ? 0.23727 0.18781 0.17097 -0.02221 -0.06839 0.02261  148 ASN A CA  
1012 C  C   . ASN A 133 ? 0.28514 0.24621 0.23628 -0.02588 -0.07547 0.02862  148 ASN A C   
1013 O  O   . ASN A 133 ? 0.27195 0.22764 0.22056 -0.03040 -0.08655 0.03240  148 ASN A O   
1014 C  CB  . ASN A 133 ? 0.26474 0.20675 0.18652 -0.02166 -0.06516 0.01692  148 ASN A CB  
1015 C  CG  . ASN A 133 ? 0.37502 0.30311 0.28394 -0.02552 -0.07559 0.01671  148 ASN A CG  
1016 O  OD1 . ASN A 133 ? 0.43107 0.34416 0.32162 -0.02576 -0.08075 0.01584  148 ASN A OD1 
1017 N  ND2 . ASN A 133 ? 0.41759 0.34916 0.33475 -0.02863 -0.07920 0.01767  148 ASN A ND2 
1018 N  N   . SER A 134 ? 0.25410 0.23014 0.22287 -0.02405 -0.06949 0.03025  149 SER A N   
1019 C  CA  . SER A 134 ? 0.24068 0.22907 0.22759 -0.02688 -0.07486 0.03724  149 SER A CA  
1020 C  C   . SER A 134 ? 0.25738 0.25260 0.25405 -0.02713 -0.08044 0.04470  149 SER A C   
1021 O  O   . SER A 134 ? 0.25722 0.25836 0.26454 -0.03153 -0.08949 0.05192  149 SER A O   
1022 C  CB  . SER A 134 ? 0.23817 0.24032 0.23965 -0.02357 -0.06590 0.03731  149 SER A CB  
1023 O  OG  . SER A 134 ? 0.30863 0.31849 0.31698 -0.01790 -0.05844 0.03815  149 SER A OG  
1024 N  N   . ILE A 135 ? 0.20433 0.19878 0.19790 -0.02274 -0.07576 0.04375  150 ILE A N   
1025 C  CA  . ILE A 135 ? 0.21195 0.21103 0.21266 -0.02239 -0.08119 0.05054  150 ILE A CA  
1026 C  C   . ILE A 135 ? 0.24520 0.23126 0.23307 -0.02799 -0.09331 0.05189  150 ILE A C   
1027 O  O   . ILE A 135 ? 0.24602 0.23720 0.24341 -0.03152 -0.10309 0.05970  150 ILE A O   
1028 C  CB  . ILE A 135 ? 0.26174 0.26059 0.25989 -0.01620 -0.07310 0.04848  150 ILE A CB  
1029 C  CG1 . ILE A 135 ? 0.24526 0.25639 0.25670 -0.01048 -0.06323 0.04876  150 ILE A CG1 
1030 C  CG2 . ILE A 135 ? 0.25990 0.25896 0.26003 -0.01582 -0.07929 0.05426  150 ILE A CG2 
1031 C  CD1 . ILE A 135 ? 0.27461 0.28173 0.28024 -0.00489 -0.05540 0.04538  150 ILE A CD1 
1032 N  N   . GLU A 136 ? 0.25819 0.22699 0.22383 -0.02867 -0.09301 0.04481  151 GLU A N   
1033 C  CA  . GLU A 136 ? 0.27604 0.22883 0.22466 -0.03294 -0.10408 0.04519  151 GLU A CA  
1034 C  C   . GLU A 136 ? 0.27820 0.22766 0.22829 -0.03981 -0.11593 0.04855  151 GLU A C   
1035 O  O   . GLU A 136 ? 0.31627 0.25828 0.26293 -0.04408 -0.12498 0.05165  151 GLU A O   
1036 C  CB  . GLU A 136 ? 0.28510 0.22043 0.20861 -0.03050 -0.09909 0.03704  151 GLU A CB  
1037 C  CG  . GLU A 136 ? 0.31836 0.25410 0.23786 -0.02541 -0.09036 0.03523  151 GLU A CG  
1038 C  CD  . GLU A 136 ? 0.46151 0.39228 0.37617 -0.02625 -0.09762 0.03962  151 GLU A CD  
1039 O  OE1 . GLU A 136 ? 0.45070 0.39307 0.38251 -0.02693 -0.10199 0.04630  151 GLU A OE1 
1040 O  OE2 . GLU A 136 ? 0.54173 0.45710 0.43516 -0.02575 -0.09872 0.03682  151 GLU A OE2 
1041 N  N   . GLU A 137 ? 0.25765 0.21230 0.21469 -0.04072 -0.11281 0.04700  152 GLU A N   
1042 C  CA  . GLU A 137 ? 0.26195 0.21325 0.22194 -0.04723 -0.12167 0.04976  152 GLU A CA  
1043 C  C   . GLU A 137 ? 0.26973 0.23719 0.25439 -0.05087 -0.12600 0.05973  152 GLU A C   
1044 O  O   . GLU A 137 ? 0.25080 0.21494 0.23927 -0.05682 -0.13210 0.06290  152 GLU A O   
1045 C  CB  . GLU A 137 ? 0.32590 0.27936 0.28705 -0.04704 -0.11749 0.04616  152 GLU A CB  
1046 C  CG  . GLU A 137 ? 0.36061 0.29590 0.29731 -0.04398 -0.11233 0.03626  152 GLU A CG  
1047 C  CD  . GLU A 137 ? 0.46130 0.40000 0.40184 -0.04316 -0.10615 0.03270  152 GLU A CD  
1048 O  OE1 . GLU A 137 ? 0.48773 0.44442 0.45014 -0.04374 -0.10317 0.03715  152 GLU A OE1 
1049 O  OE2 . GLU A 137 ? 0.55325 0.47661 0.47458 -0.04138 -0.10403 0.02580  152 GLU A OE2 
1050 N  N   . ARG A 138 ? 0.23014 0.21435 0.23118 -0.04708 -0.12257 0.06525  153 ARG A N   
1051 C  CA  . ARG A 138 ? 0.22226 0.22449 0.24819 -0.04889 -0.12418 0.07531  153 ARG A CA  
1052 C  C   . ARG A 138 ? 0.23077 0.23375 0.25965 -0.04907 -0.12862 0.08024  153 ARG A C   
1053 O  O   . ARG A 138 ? 0.24884 0.26886 0.29889 -0.04848 -0.12803 0.08896  153 ARG A O   
1054 C  CB  . ARG A 138 ? 0.19363 0.21748 0.23948 -0.04283 -0.11461 0.07876  153 ARG A CB  
1055 C  CG  . ARG A 138 ? 0.23192 0.25807 0.28039 -0.04456 -0.11186 0.07662  153 ARG A CG  
1056 C  CD  . ARG A 138 ? 0.25540 0.29746 0.31639 -0.03744 -0.10060 0.07678  153 ARG A CD  
1057 N  NE  . ARG A 138 ? 0.28073 0.32563 0.34581 -0.04028 -0.09937 0.07607  153 ARG A NE  
1058 C  CZ  . ARG A 138 ? 0.31126 0.34210 0.35977 -0.04120 -0.09688 0.06673  153 ARG A CZ  
1059 N  NH1 . ARG A 138 ? 0.28829 0.30275 0.31583 -0.03890 -0.09401 0.05752  153 ARG A NH1 
1060 N  NH2 . ARG A 138 ? 0.31531 0.34922 0.36891 -0.04423 -0.09709 0.06736  153 ARG A NH2 
1061 N  N   . ARG A 139 ? 0.23530 0.22005 0.24297 -0.04958 -0.13260 0.07510  154 ARG A N   
1062 C  CA  . ARG A 139 ? 0.24462 0.22806 0.25302 -0.05018 -0.13753 0.07928  154 ARG A CA  
1063 C  C   . ARG A 139 ? 0.27965 0.23818 0.26196 -0.05375 -0.14437 0.07355  154 ARG A C   
1064 O  O   . ARG A 139 ? 0.31286 0.26613 0.29188 -0.05541 -0.15000 0.07623  154 ARG A O   
1065 C  CB  . ARG A 139 ? 0.26394 0.25679 0.27693 -0.04224 -0.13057 0.08000  154 ARG A CB  
1066 C  CG  . ARG A 139 ? 0.30181 0.28183 0.29362 -0.03789 -0.12535 0.07139  154 ARG A CG  
1067 C  CD  . ARG A 139 ? 0.36849 0.35802 0.36701 -0.03023 -0.11832 0.07335  154 ARG A CD  
1068 N  NE  . ARG A 139 ? 0.34363 0.31924 0.32181 -0.02672 -0.11029 0.06427  154 ARG A NE  
1069 C  CZ  . ARG A 139 ? 0.49971 0.47815 0.47906 -0.02049 -0.10108 0.06265  154 ARG A CZ  
1070 N  NH1 . ARG A 139 ? 0.48617 0.47914 0.48385 -0.01588 -0.09811 0.06855  154 ARG A NH1 
1071 N  NH2 . ARG A 139 ? 0.50491 0.47093 0.46628 -0.01860 -0.09478 0.05547  154 ARG A NH2 
1072 O  OXT . ARG A 139 ? 0.28074 0.22383 0.24447 -0.05436 -0.14381 0.06622  154 ARG A OXT 
1073 N  N   . TPO B 3   ? 0.35088 0.41086 0.36659 -0.00244 0.03585  0.02768  641 TPO B N   
1074 C  CA  . TPO B 3   ? 0.35180 0.41753 0.37936 -0.00905 0.03129  0.03122  641 TPO B CA  
1075 C  CB  . TPO B 3   ? 0.38658 0.45633 0.42010 -0.01495 0.02950  0.03810  641 TPO B CB  
1076 C  CG2 . TPO B 3   ? 0.45306 0.52635 0.49726 -0.02228 0.02315  0.04177  641 TPO B CG2 
1077 O  OG1 . TPO B 3   ? 0.50765 0.58716 0.54431 -0.01153 0.03625  0.04551  641 TPO B OG1 
1078 P  P   . TPO B 3   ? 0.81949 0.91786 0.87365 -0.01291 0.03937  0.05796  641 TPO B P   
1079 O  O1P . TPO B 3   ? 0.64682 0.74823 0.70571 -0.01074 0.03864  0.05563  641 TPO B O1P 
1080 O  O2P . TPO B 3   ? 0.59518 0.70030 0.64606 -0.00509 0.04919  0.06300  641 TPO B O2P 
1081 O  O3P . TPO B 3   ? 0.58382 0.68415 0.64691 -0.02309 0.03245  0.06411  641 TPO B O3P 
1082 C  C   . TPO B 3   ? 0.28226 0.33846 0.30641 -0.01224 0.02495  0.02411  641 TPO B C   
1083 O  O   . TPO B 3   ? 0.42189 0.48029 0.45155 -0.01399 0.02234  0.02387  641 TPO B O   
1084 N  N   . ILE B 4   ? 0.20500 0.25116 0.22021 -0.01247 0.02276  0.01885  642 ILE B N   
1085 C  CA  . ILE B 4   ? 0.17972 0.21855 0.19267 -0.01461 0.01779  0.01340  642 ILE B CA  
1086 C  C   . ILE B 4   ? 0.19512 0.23213 0.20511 -0.01071 0.01872  0.00868  642 ILE B C   
1087 O  O   . ILE B 4   ? 0.16833 0.20334 0.17974 -0.01213 0.01574  0.00613  642 ILE B O   
1088 C  CB  . ILE B 4   ? 0.16854 0.19849 0.17479 -0.01602 0.01494  0.01048  642 ILE B CB  
1089 C  CG1 . ILE B 4   ? 0.17453 0.19845 0.17995 -0.01822 0.01035  0.00714  642 ILE B CG1 
1090 C  CG2 . ILE B 4   ? 0.15517 0.18078 0.15366 -0.01189 0.01673  0.00680  642 ILE B CG2 
1091 C  CD1 . ILE B 4   ? 0.16625 0.18187 0.16624 -0.01941 0.00751  0.00576  642 ILE B CD1 
1092 N  N   . GLU B 5   ? 0.20384 0.24030 0.20855 -0.00576 0.02250  0.00769  643 GLU B N   
1093 C  CA  . GLU B 5   ? 0.16697 0.19990 0.16774 -0.00241 0.02254  0.00359  643 GLU B CA  
1094 C  C   . GLU B 5   ? 0.21019 0.24988 0.21670 -0.00012 0.02505  0.00601  643 GLU B C   
1095 O  O   . GLU B 5   ? 0.24376 0.28331 0.24621 0.00534  0.02882  0.00621  643 GLU B O   
1096 C  CB  . GLU B 5   ? 0.30314 0.32886 0.29298 0.00162  0.02387  0.00109  643 GLU B CB  
1097 C  CG  . GLU B 5   ? 0.26186 0.28145 0.24701 -0.00069 0.02063  -0.00090 643 GLU B CG  
1098 C  CD  . GLU B 5   ? 0.44645 0.45760 0.42016 0.00251  0.02026  -0.00323 643 GLU B CD  
1099 O  OE1 . GLU B 5   ? 0.52867 0.53553 0.49712 0.00562  0.02036  -0.00528 643 GLU B OE1 
1100 O  OE2 . GLU B 5   ? 0.50952 0.51705 0.47851 0.00181  0.01924  -0.00293 643 GLU B OE2 
1101 N  N   . GLU B 6   ? 0.19168 0.23635 0.20690 -0.00413 0.02254  0.00807  644 GLU B N   
1102 C  CA  . GLU B 6   ? 0.18887 0.24072 0.21154 -0.00313 0.02349  0.01093  644 GLU B CA  
1103 C  C   . GLU B 6   ? 0.15885 0.20833 0.18417 -0.00718 0.01838  0.00866  644 GLU B C   
1104 O  O   . GLU B 6   ? 0.14642 0.19077 0.16961 -0.01107 0.01470  0.00682  644 GLU B O   
1105 C  CB  . GLU B 6   ? 0.23436 0.29726 0.26692 -0.00454 0.02546  0.01874  644 GLU B CB  
1106 C  CG  . GLU B 6   ? 0.30273 0.37185 0.33510 0.00195  0.03254  0.02282  644 GLU B CG  
1107 C  CD  . GLU B 6   ? 0.43450 0.51757 0.48004 0.00008  0.03441  0.03233  644 GLU B CD  
1108 O  OE1 . GLU B 6   ? 0.43609 0.52165 0.48934 -0.00745 0.02885  0.03520  644 GLU B OE1 
1109 O  OE2 . GLU B 6   ? 0.46837 0.55950 0.51615 0.00628  0.04121  0.03742  644 GLU B OE2 
1110 N  N   . VAL B 7   ? 0.14061 0.19324 0.16965 -0.00560 0.01842  0.00907  645 VAL B N   
1111 C  CA  . VAL B 7   ? 0.14964 0.19995 0.18038 -0.00902 0.01379  0.00744  645 VAL B CA  
1112 C  C   . VAL B 7   ? 0.15939 0.21524 0.19837 -0.01394 0.01042  0.01266  645 VAL B C   
1113 O  O   . VAL B 7   ? 0.16632 0.23125 0.21319 -0.01410 0.01222  0.01875  645 VAL B O   
1114 C  CB  . VAL B 7   ? 0.13049 0.18033 0.16062 -0.00556 0.01448  0.00549  645 VAL B CB  
1115 C  CG1 . VAL B 7   ? 0.13493 0.17662 0.15603 -0.00280 0.01526  0.00034  645 VAL B CG1 
1116 C  CG2 . VAL B 7   ? 0.12067 0.17875 0.15655 -0.00128 0.01835  0.00989  645 VAL B CG2 
1117 N  N   . ASP B 8   ? 0.15276 0.20265 0.18943 -0.01802 0.00518  0.01085  646 ASP B N   
1118 C  CA  . ASP B 8   ? 0.17861 0.23029 0.22068 -0.02359 -0.00013 0.01541  646 ASP B CA  
1119 C  C   . ASP B 8   ? 0.19731 0.25135 0.24328 -0.02413 -0.00290 0.01652  646 ASP B C   
1120 O  O   . ASP B 8   ? 0.18786 0.24419 0.23932 -0.02894 -0.00814 0.02118  646 ASP B O   
1121 C  CB  . ASP B 8   ? 0.16909 0.20935 0.20287 -0.02757 -0.00503 0.01283  646 ASP B CB  
1122 C  CG  . ASP B 8   ? 0.23743 0.27542 0.26819 -0.02764 -0.00320 0.01266  646 ASP B CG  
1123 O  OD1 . ASP B 8   ? 0.27040 0.31561 0.30803 -0.02936 -0.00223 0.01810  646 ASP B OD1 
1124 O  OD2 . ASP B 8   ? 0.24049 0.27027 0.26261 -0.02579 -0.00255 0.00776  646 ASP B OD2 
1125 O  OXT . ASP B 8   ? 0.14914 0.20233 0.19276 -0.02023 -0.00069 0.01322  646 ASP B OXT 
1126 CL CL  . CL  C .   ? 0.25507 0.26609 0.25956 -0.00956 -0.01080 0.00213  201 CL  A CL  
1127 O  O   . HOH D .   ? 0.25716 0.24911 0.20563 0.05044  0.04154  0.00589  301 HOH A O   
1128 O  O   . HOH D .   ? 0.52255 0.54472 0.54617 -0.02654 -0.04851 0.02096  302 HOH A O   
1129 O  O   . HOH D .   ? 0.44992 0.45141 0.45724 -0.03026 -0.03930 0.01181  303 HOH A O   
1130 O  O   . HOH D .   ? 0.33911 0.28871 0.29905 -0.02077 -0.03784 -0.00795 304 HOH A O   
1131 O  O   . HOH D .   ? 0.23630 0.25554 0.25725 -0.03522 -0.03186 0.01191  305 HOH A O   
1132 O  O   . HOH D .   ? 0.55976 0.53015 0.51806 -0.00011 -0.02197 0.02014  306 HOH A O   
1133 O  O   . HOH D .   ? 0.67072 0.57008 0.55377 -0.03448 -0.10470 0.02394  307 HOH A O   
1134 O  O   . HOH D .   ? 0.29938 0.24101 0.25291 -0.03333 -0.03093 -0.00185 308 HOH A O   
1135 O  O   . HOH D .   ? 0.31117 0.29006 0.27564 -0.00342 -0.02884 0.02068  309 HOH A O   
1136 O  O   . HOH D .   ? 0.25290 0.22167 0.22206 -0.02524 -0.01897 -0.00552 310 HOH A O   
1137 O  O   . HOH D .   ? 0.16414 0.18892 0.17743 -0.01802 0.00233  -0.00124 311 HOH A O   
1138 O  O   . HOH D .   ? 0.20913 0.17374 0.18324 -0.03446 -0.02307 0.00293  312 HOH A O   
1139 O  O   . HOH D .   ? 0.26619 0.29594 0.23930 -0.00121 0.03685  0.02673  313 HOH A O   
1140 O  O   . HOH D .   ? 0.26150 0.24294 0.22890 0.02620  0.01636  -0.00163 314 HOH A O   
1141 O  O   . HOH D .   ? 0.35055 0.30801 0.26391 0.03718  0.02368  -0.01632 315 HOH A O   
1142 O  O   . HOH D .   ? 0.17782 0.21065 0.19986 -0.01260 0.00258  0.00459  316 HOH A O   
1143 O  O   . HOH D .   ? 0.35448 0.35450 0.29582 0.05574  0.05136  0.01275  317 HOH A O   
1144 O  O   . HOH D .   ? 0.40527 0.31388 0.32981 -0.05451 -0.15227 0.06124  318 HOH A O   
1145 O  O   . HOH D .   ? 0.27697 0.21378 0.19907 0.02700  0.00133  -0.02226 319 HOH A O   
1146 O  O   . HOH D .   ? 0.26787 0.37609 0.37134 -0.00074 -0.00332 0.04321  320 HOH A O   
1147 O  O   . HOH D .   ? 0.33711 0.31571 0.28961 -0.01478 0.00354  0.01691  321 HOH A O   
1148 O  O   . HOH D .   ? 0.32983 0.31918 0.31624 0.02256  -0.00061 0.01501  322 HOH A O   
1149 O  O   . HOH D .   ? 0.35508 0.37621 0.30680 -0.00007 0.04174  0.03709  323 HOH A O   
1150 O  O   . HOH D .   ? 0.20411 0.18993 0.17184 -0.01029 -0.00629 -0.00992 324 HOH A O   
1151 O  O   . HOH D .   ? 0.32405 0.19424 0.22544 -0.03237 -0.04667 -0.00294 325 HOH A O   
1152 O  O   . HOH D .   ? 0.55792 0.50436 0.43148 0.00447  0.00996  0.01582  326 HOH A O   
1153 O  O   . HOH D .   ? 0.31297 0.33044 0.26785 0.07996  0.06494  0.01057  327 HOH A O   
1154 O  O   . HOH D .   ? 0.36901 0.32994 0.35345 -0.05573 -0.04287 0.01843  328 HOH A O   
1155 O  O   . HOH D .   ? 0.23414 0.21488 0.17554 0.00070  0.00207  -0.00048 329 HOH A O   
1156 O  O   . HOH D .   ? 0.29554 0.22603 0.25585 -0.06379 -0.13975 0.05499  330 HOH A O   
1157 O  O   . HOH D .   ? 0.24579 0.26113 0.26181 -0.01897 -0.01014 0.00272  331 HOH A O   
1158 O  O   . HOH D .   ? 0.23211 0.12079 0.12374 0.01688  -0.00747 -0.01547 332 HOH A O   
1159 O  O   . HOH D .   ? 0.17691 0.17666 0.17686 0.00743  -0.00134 -0.00849 333 HOH A O   
1160 O  O   . HOH D .   ? 0.42135 0.29815 0.33819 -0.03884 -0.04369 0.01194  334 HOH A O   
1161 O  O   . HOH D .   ? 0.32623 0.34865 0.30429 0.03371  0.03868  0.00086  335 HOH A O   
1162 O  O   . HOH D .   ? 0.24190 0.30909 0.29320 -0.00220 0.00937  0.02647  336 HOH A O   
1163 O  O   . HOH D .   ? 0.16339 0.15780 0.15943 -0.01000 -0.00970 -0.00845 337 HOH A O   
1164 O  O   . HOH D .   ? 0.50166 0.45588 0.45408 -0.00753 -0.00806 0.01205  338 HOH A O   
1165 O  O   . HOH D .   ? 0.26612 0.25934 0.23268 -0.00689 0.00005  -0.00218 339 HOH A O   
1166 O  O   . HOH D .   ? 0.21425 0.20542 0.19990 -0.01977 -0.00709 -0.00610 340 HOH A O   
1167 O  O   . HOH D .   ? 0.28688 0.31300 0.28454 -0.03446 0.01631  0.04985  341 HOH A O   
1168 O  O   . HOH D .   ? 0.32947 0.26177 0.22674 -0.01281 -0.04821 0.01295  342 HOH A O   
1169 O  O   . HOH D .   ? 0.26786 0.25209 0.24971 -0.03310 -0.03974 0.00327  343 HOH A O   
1170 O  O   . HOH D .   ? 0.17478 0.21313 0.19849 -0.00859 0.00695  0.00593  344 HOH A O   
1171 O  O   . HOH D .   ? 0.24317 0.32560 0.32151 0.00321  -0.00357 0.02821  345 HOH A O   
1172 O  O   . HOH D .   ? 0.32923 0.37817 0.37031 0.01772  -0.00232 0.03285  346 HOH A O   
1173 O  O   . HOH D .   ? 0.13359 0.23569 0.21851 0.00422  0.01567  0.03546  347 HOH A O   
1174 O  O   . HOH D .   ? 0.42211 0.35749 0.38121 -0.05192 -0.02759 0.03843  348 HOH A O   
1175 O  O   . HOH D .   ? 0.22912 0.20587 0.15083 0.00052  0.01422  0.00831  349 HOH A O   
1176 O  O   . HOH D .   ? 0.28750 0.28230 0.23279 -0.01002 0.02041  0.02485  350 HOH A O   
1177 O  O   . HOH D .   ? 0.27857 0.30722 0.32113 -0.02545 -0.10127 0.07759  351 HOH A O   
1178 O  O   . HOH D .   ? 0.27059 0.19463 0.18873 0.02903  -0.00398 -0.02298 352 HOH A O   
1179 O  O   . HOH D .   ? 0.25356 0.22774 0.19302 0.01885  0.01814  -0.00842 353 HOH A O   
1180 O  O   . HOH D .   ? 0.34832 0.28000 0.24774 0.06436  0.02609  -0.01900 354 HOH A O   
1181 O  O   . HOH D .   ? 0.32795 0.35671 0.34581 -0.04257 0.00331  0.04322  355 HOH A O   
1182 O  O   . HOH D .   ? 0.37387 0.43710 0.37863 -0.00816 0.04480  0.05115  356 HOH A O   
1183 O  O   . HOH D .   ? 0.42483 0.48228 0.45610 0.02533  0.02707  0.02457  357 HOH A O   
1184 O  O   . HOH D .   ? 0.37779 0.29364 0.29516 -0.04427 -0.13261 0.05028  358 HOH A O   
1185 O  O   . HOH D .   ? 0.32842 0.29460 0.28467 -0.02516 -0.06307 0.01926  359 HOH A O   
1186 O  O   . HOH D .   ? 0.22566 0.23114 0.19073 -0.00359 0.01856  0.00438  360 HOH A O   
1187 O  O   . HOH D .   ? 0.48160 0.48630 0.41506 0.07291  0.06435  0.00692  361 HOH A O   
1188 O  O   . HOH D .   ? 0.15929 0.17841 0.15859 -0.02774 0.01033  0.02592  362 HOH A O   
1189 O  O   . HOH D .   ? 0.38557 0.43825 0.44479 -0.06052 -0.01671 0.05677  363 HOH A O   
1190 O  O   . HOH D .   ? 0.20751 0.12544 0.12338 0.02268  0.00261  -0.01145 364 HOH A O   
1191 O  O   . HOH D .   ? 0.16911 0.18809 0.18033 -0.01091 -0.00013 -0.00446 365 HOH A O   
1192 O  O   . HOH D .   ? 0.19305 0.17923 0.15275 0.03565  0.02698  -0.00071 366 HOH A O   
1193 O  O   . HOH D .   ? 0.18170 0.16893 0.13725 0.03529  0.02920  -0.00113 367 HOH A O   
1194 O  O   . HOH D .   ? 0.37931 0.35994 0.34252 -0.00846 -0.01184 -0.01085 368 HOH A O   
1195 O  O   . HOH D .   ? 0.48249 0.53638 0.54844 -0.04245 -0.05657 0.03917  369 HOH A O   
1196 O  O   . HOH D .   ? 0.28866 0.32817 0.29603 0.01781  0.02831  0.01251  370 HOH A O   
1197 O  O   . HOH D .   ? 0.35609 0.39394 0.40031 -0.01685 -0.06568 0.05697  371 HOH A O   
1198 O  O   . HOH D .   ? 0.35830 0.29541 0.27031 0.01771  -0.00157 -0.02197 372 HOH A O   
1199 O  O   . HOH D .   ? 0.32810 0.21446 0.23433 0.00456  -0.01672 -0.00503 373 HOH A O   
1200 O  O   . HOH D .   ? 0.29252 0.27008 0.27744 -0.04234 -0.01351 0.02577  374 HOH A O   
1201 O  O   . HOH D .   ? 0.31187 0.32469 0.28059 0.02621  0.03355  -0.00309 375 HOH A O   
1202 O  O   . HOH D .   ? 0.24349 0.25293 0.25623 -0.03823 -0.04830 0.01571  376 HOH A O   
1203 O  O   . HOH D .   ? 0.47929 0.38230 0.38157 -0.01659 -0.03227 -0.01465 377 HOH A O   
1204 O  O   . HOH D .   ? 0.35265 0.27832 0.24870 0.04015  0.01093  -0.02334 378 HOH A O   
1205 O  O   . HOH D .   ? 0.32650 0.31847 0.31355 -0.03040 -0.04387 0.00750  379 HOH A O   
1206 O  O   . HOH D .   ? 0.41272 0.40389 0.38620 -0.01135 -0.01431 -0.00428 380 HOH A O   
1207 O  O   . HOH D .   ? 0.18378 0.13944 0.12638 0.02749  0.01412  -0.00748 381 HOH A O   
1208 O  O   . HOH D .   ? 0.23952 0.26596 0.27218 -0.03005 -0.03103 0.01983  382 HOH A O   
1209 O  O   . HOH D .   ? 0.18510 0.30994 0.29249 0.01102  0.01816  0.04918  383 HOH A O   
1210 O  O   . HOH D .   ? 0.46895 0.32601 0.31055 0.01965  -0.01382 -0.02361 384 HOH A O   
1211 O  O   . HOH D .   ? 0.29703 0.23077 0.22581 -0.01833 -0.02614 -0.01216 385 HOH A O   
1212 O  O   . HOH D .   ? 0.23098 0.20197 0.20211 -0.02874 -0.02508 -0.00401 386 HOH A O   
1213 O  O   . HOH D .   ? 0.30121 0.32107 0.28173 0.03008  0.03468  0.00866  387 HOH A O   
1214 O  O   . HOH D .   ? 0.40052 0.45624 0.44046 0.01510  0.01176  0.02461  388 HOH A O   
1215 O  O   . HOH D .   ? 0.21500 0.20953 0.20922 -0.02875 -0.01041 0.00264  389 HOH A O   
1216 O  O   . HOH D .   ? 0.42088 0.25034 0.28066 -0.00243 -0.03612 -0.01196 390 HOH A O   
1217 O  O   . HOH D .   ? 0.48718 0.49043 0.50719 -0.04736 -0.09538 0.05000  391 HOH A O   
1218 O  O   . HOH D .   ? 0.22024 0.31842 0.30645 -0.01178 0.00541  0.03680  392 HOH A O   
1219 O  O   . HOH D .   ? 0.29549 0.25152 0.19371 0.00226  0.00409  0.00466  393 HOH A O   
1220 O  O   . HOH D .   ? 0.48008 0.39441 0.36780 -0.01009 -0.03132 -0.01190 394 HOH A O   
1221 O  O   . HOH D .   ? 0.44485 0.50575 0.48418 0.02219  0.02131  0.02688  395 HOH A O   
1222 O  O   . HOH D .   ? 0.37734 0.34703 0.32434 -0.01146 -0.00276 0.01532  396 HOH A O   
1223 O  O   . HOH D .   ? 0.31342 0.36312 0.35980 0.01007  -0.01798 0.04037  397 HOH A O   
1224 O  O   . HOH D .   ? 0.41613 0.31495 0.27299 -0.01542 -0.07148 0.02318  398 HOH A O   
1225 O  O   . HOH D .   ? 0.47670 0.33557 0.34392 -0.00812 -0.03506 -0.01822 399 HOH A O   
1226 O  O   . HOH D .   ? 0.32658 0.34583 0.34824 -0.03667 -0.02774 0.01199  400 HOH A O   
1227 O  O   . HOH D .   ? 0.46666 0.43147 0.42630 -0.03316 -0.04814 0.00217  401 HOH A O   
1228 O  O   . HOH D .   ? 0.43784 0.43356 0.43557 -0.00139 -0.07170 0.05911  402 HOH A O   
1229 O  O   . HOH D .   ? 0.20413 0.25902 0.24298 -0.00820 0.00905  0.01917  403 HOH A O   
1230 O  O   . HOH D .   ? 0.39248 0.37522 0.35620 -0.00952 -0.01293 -0.00856 404 HOH A O   
1231 O  O   . HOH D .   ? 0.19937 0.20831 0.20751 -0.01346 -0.00684 -0.00388 405 HOH A O   
1232 O  O   . HOH D .   ? 0.52143 0.40888 0.40296 -0.04259 -0.12785 0.03684  406 HOH A O   
1233 O  O   . HOH D .   ? 0.51189 0.62004 0.61152 -0.05641 0.00137  0.08817  407 HOH A O   
1234 O  O   . HOH D .   ? 0.22203 0.23078 0.23091 -0.00043 -0.00425 -0.00539 408 HOH A O   
1235 O  O   . HOH D .   ? 0.32962 0.32518 0.28961 -0.00348 0.01003  -0.00248 409 HOH A O   
1236 O  O   . HOH D .   ? 0.36463 0.29147 0.24790 0.04781  0.02061  -0.02145 410 HOH A O   
1237 O  O   . HOH D .   ? 0.25726 0.24134 0.17940 -0.00012 0.02279  0.01858  411 HOH A O   
1238 O  O   . HOH D .   ? 0.58286 0.47547 0.47298 -0.04439 -0.12455 0.03325  412 HOH A O   
1239 O  O   . HOH D .   ? 0.46369 0.47253 0.46039 -0.04002 0.00317  0.04069  413 HOH A O   
1240 O  O   . HOH D .   ? 0.18779 0.28997 0.26250 0.01513  0.02981  0.03505  414 HOH A O   
1241 O  O   . HOH D .   ? 0.52947 0.43324 0.45211 0.00284  -0.01456 0.00237  415 HOH A O   
1242 O  O   . HOH D .   ? 0.25773 0.34938 0.32179 0.00734  0.02757  0.02968  416 HOH A O   
1243 O  O   . HOH D .   ? 0.48140 0.55564 0.49849 -0.01850 0.04442  0.06897  417 HOH A O   
1244 O  O   . HOH D .   ? 0.36642 0.42970 0.40462 0.01269  0.02272  0.02430  418 HOH A O   
1245 O  O   . HOH D .   ? 0.47958 0.34045 0.37628 -0.04317 -0.06037 -0.00081 419 HOH A O   
1246 O  O   . HOH D .   ? 0.40538 0.24825 0.28120 0.00307  -0.02909 -0.00527 420 HOH A O   
1247 O  O   . HOH D .   ? 0.38558 0.32753 0.35759 -0.06336 -0.13156 0.05232  421 HOH A O   
1248 O  O   . HOH D .   ? 0.37051 0.27641 0.21601 -0.00184 -0.03025 0.00629  422 HOH A O   
1249 O  O   . HOH D .   ? 0.30643 0.30710 0.30003 -0.03583 -0.00068 0.02735  423 HOH A O   
1250 O  O   . HOH D .   ? 0.37196 0.35985 0.31949 -0.01654 0.01391  0.02880  424 HOH A O   
1251 O  O   . HOH D .   ? 0.39286 0.28168 0.29833 -0.05612 -0.13706 0.03837  425 HOH A O   
1252 O  O   . HOH D .   ? 0.56529 0.47661 0.43179 -0.00938 -0.04518 0.00510  426 HOH A O   
1253 O  O   . HOH D .   ? 0.50104 0.40566 0.42259 0.01913  -0.00936 0.00330  427 HOH A O   
1254 O  O   . HOH D .   ? 0.45285 0.44970 0.45714 -0.04534 -0.05381 0.01576  428 HOH A O   
1255 O  O   . HOH D .   ? 0.22816 0.16116 0.15118 0.01383  -0.00961 -0.02231 429 HOH A O   
1256 O  O   . HOH D .   ? 0.38596 0.44241 0.40997 0.02105  0.03101  0.02252  430 HOH A O   
1257 O  O   . HOH D .   ? 0.53619 0.37250 0.39618 -0.02672 -0.05733 -0.01329 431 HOH A O   
1258 O  O   . HOH D .   ? 0.19306 0.14482 0.12466 0.03494  0.01944  -0.00821 432 HOH A O   
1259 O  O   . HOH D .   ? 0.36820 0.28688 0.24479 0.00680  -0.01064 -0.01205 433 HOH A O   
1260 O  O   . HOH D .   ? 0.29167 0.21002 0.18835 0.02507  -0.00334 -0.02482 434 HOH A O   
1261 O  O   . HOH D .   ? 0.37375 0.35397 0.30731 0.00998  0.01292  0.00018  435 HOH A O   
1262 O  O   . HOH D .   ? 0.60791 0.66580 0.65647 0.04910  0.02074  0.02148  436 HOH A O   
1263 O  O   . HOH D .   ? 0.36262 0.28546 0.23707 -0.00724 -0.03554 0.01202  437 HOH A O   
1264 O  O   . HOH E .   ? 0.26821 0.32777 0.30759 -0.02130 0.01391  0.02506  701 HOH B O   
1265 O  O   . HOH E .   ? 0.46719 0.51061 0.51363 -0.04084 -0.02092 0.02491  702 HOH B O   
1266 O  O   . HOH E .   ? 0.27363 0.28785 0.24708 -0.00143 0.02247  0.00421  703 HOH B O   
1267 O  O   . HOH E .   ? 0.24364 0.24953 0.24702 -0.02840 -0.00977 0.00292  704 HOH B O   
1268 O  O   . HOH E .   ? 0.31887 0.38556 0.35198 0.00796  0.03105  0.01723  705 HOH B O   
1269 O  O   . HOH E .   ? 0.39310 0.40855 0.40865 -0.03628 -0.01103 0.01441  706 HOH B O   
1270 O  O   . HOH E .   ? 0.43118 0.49464 0.45105 0.02270  0.04182  0.01779  707 HOH B O   
# 
